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{{Short description|English biochemist and crystallographer}}
{{For|the Industrial Revolution-era designer|John Kendrew (inventor)}}
{{For|the Industrial Revolution-era designer|John Kendrew (inventor)}}
{{Use dmy dates|date=May 2012}}
{{Use dmy dates|date=June 2021}}
{{Use British English|date=May 2012}}
{{Use British English|date=May 2012}}
{{Infobox scientist
{{Infobox scientist
| image = John Kendrew Nobel.jpg
| image = John Kendrew Nobel.jpg
| honorific_suffix = {{post-nominals|size=100%|country=GBR|CBE|FRS}}
| honorific_suffix = {{post-nominals|size=100%|country=GBR|CBE|FRS}}
| image_size = 200px
| image_size = 200px
| caption = John Kendrew
| birth_name = John Cowdery Kendrew
|birth_name = John Cowdery Kendrew
| birth_date = {{birth date|1917|3|24|df=yes}}
⚫
| birth_place = [[Oxford]], England
| birth_date = {{birth date|1917|3|24|df=yes}}
| death_date = {{death date and age|1997|8|23|1917|3|24|df=yes}}
⚫
| birth_place = [[Oxford]], [[Oxfordshire]], [[England]]
⚫
| death_place = [[Cambridge]], England
| death_date = {{death date and age|1997|8|23|1917|3|24|df=yes}}
| field = [[Crystallography]]
⚫
| death_place = [[Cambridge]], [[Cambridgeshire]], [[England]]
⚫
| work_institution = [[MRC Laboratory of Molecular Biology]]<br>[[Peterhouse, Cambridge]]<br>[[Royal Air Force]]
| nationality = British
| field = [[Crystallography]]
| education = [[Clifton College]], [[University of Cambridge]]
⚫
| work_institution = [[Peterhouse, Cambridge]]<br>[[Royal Air Force]]
| education = [[Clifton College]]
| alma_mater = [[University of Cambridge]]
| doctoral_advisor =
| doctoral_advisor =
| thesis_title = X-ray studies of certain crystalline proteins : the crystal structure of foetal and adult sheep haemoglobins and of horse myoglobin
| thesis_title = X-ray studies of certain crystalline proteins : the crystal structure of foetal and adult sheep haemoglobins and of horse myoglobin
| thesis_year= 1949
| thesis_year = 1949
| thesis_url = http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648050
| thesis_url = http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648050
| notable_students = [[James D. Watson]] (postdoc)<ref name=atree/>
| notable_students = [[James D. Watson]] (postdoc)<ref name=atree/>
| academic_advisors = [[Max Perutz]]
| academic_advisors = [[Max Perutz]]
| doctoral_students = {{Plainlist|
| doctoral_students = {{Plainlist|
* [[Hugh Huxley]]<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Investigations of biological structures by X-ray methods : the structure of muscle|first= Hugh Esmor|last=Huxley|date=1953|url=http://ulmss-newton.lib.cam.ac.uk/vwebv/holdingsInfo?bibId=35871|id={{EThOS|uk.bl.ethos.604904}}|website=lib.cam.ac.uk|oclc=885437514}}</ref><ref name=atree>{{cite web|url=https://academictree.org/chemistry/peopleinfo.php?pid=1944|website=academictree.org|title=John Kendrew academic geneaology}}</ref>
* [[Hugh Huxley]]<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Investigations of biological structures by X-ray methods : the structure of muscle|first=Hugh Esmor|last=Huxley|date=1953|url=http://ulmss-newton.lib.cam.ac.uk/vwebv/holdingsInfo?bibId=35871|id={{EThOS|uk.bl.ethos.604904}}|website=lib.cam.ac.uk|oclc=885437514|access-date=4 December 2017|archive-date=19 May 2022|archive-url=https://web.archive.org/web/20220519183634/https://ulmss-newton.lib.cam.ac.uk/vwebv/holdingsInfo?bibId=35871|url-status=dead}}</ref><ref name=atree>{{cite web|url=https://academictree.org/chemistry/peopleinfo.php?pid=1944|website=academictree.org|title=John Kendrew academic genealogy}}</ref>
* [[Lubert Stryer]]<ref name=atree/>}}
* [[Lubert Stryer]]<ref name=atree/>}}
| known_for = [[Heme]]-containing [[protein]]s
| known_for = [[Heme|Haem]]-containing [[protein]]s
| prizes = {{Plainlist|
| prizes = {{Plainlist|
* [[Nobel Prize for Chemistry]] {{small|(1962)}}
* [[Nobel Prize for Chemistry]] (1962)
* [[EMBO Member]] {{small|(1964)}}
* [[Royal Medal]] (1965)}}
| module = {{Infobox military person | embed=yes
* [[Royal Medal]] {{small|(1965)}}}}
|nickname=
|allegiance= {{flag|United Kingdom}}
|branch= {{air force|United Kingdom}}
|serviceyears= 1941–1945
|rank=[[Wing commander|Wing Commander]] ([[Royal Air Force Volunteer Reserve|RAFVR]])
|unit=
|commands=
|battles=[[Second World War]]
|awards=
|relations=
|signature = }}
}}
}}


'''Sir John Cowdery Kendrew''', {{post-nominals|country=GBR|CBE|FRS}}<ref name="frs">{{Cite journal | last1 = Holmes | first1 = K. C. | doi = 10.1098/rsbm.2001.0018 | title = Sir John Cowdery Kendrew. 24 March 1917 - 23 August 1997: Elected F.R.S. 1960 | journal = [[Biographical Memoirs of Fellows of the Royal Society]] | volume = 47 | pages = 311–332 | year = 2001 | pmid = 15124647| doi-access = free }}</ref> (24 March 1917 &ndash; 23 August 1997) was an [[England|English]] [[biochemist]], [[crystallography|crystallographer]], and science administrator. Kendrew shared the 1962 [[Nobel Prize in Chemistry]] with [[Max Perutz]], for their work at the [[Cavendish Laboratory]] to investigate the structure of [[heme]]-containing [[protein]]s.
'''Sir John Cowdery Kendrew''', {{post-nominals|country=GBR|CBE|FRS}}<ref name="frs">{{Cite journal | last1 = Holmes | first1 = K. C. | doi = 10.1098/rsbm.2001.0018 | title = Sir John Cowdery Kendrew. 24 March 1917 - 23 August 1997: Elected F.R.S. 1960 | journal = [[Biographical Memoirs of Fellows of the Royal Society]] | volume = 47 | pages = 311–332 | year = 2001 | pmid = 15124647| doi-access = free | hdl = 11858/00-001M-0000-0028-EC77-7 | hdl-access = free }}</ref> (24 March 1917 &ndash; 23 August 1997) was an [[England|English]] [[biochemist]], [[crystallography|crystallographer]], and science administrator. Kendrew shared the 1962 [[Nobel Prize in Chemistry]] with [[Max Perutz]], for their work at the [[Cavendish Laboratory]] to investigate the structure of [[heme|haem]]-containing [[protein]]s.


==Education and early life==
==Education and early life==
Kendrew was born in [[Oxford]], son of [[Wilfrid George Kendrew]], [[reader (academic rank)|reader]] in [[climatology]] in the [[University of Oxford]], and Evelyn May Graham Sandburg, art historian. After prep school at the [[Dragon School]] in Oxford, he was educated at [[Clifton College]]<ref>"Clifton College Register" Muirhead, J.A.O. p462: Bristol; J.W Arrowsmith for Old Cliftonian Society; April, 1948</ref> in [[Bristol]], 1930–1936. He attended [[Trinity College, Cambridge|Trinity College]], [[University of Cambridge|Cambridge]] in 1936, as a Major Scholar, graduating in chemistry in 1939. He spent the early months of [[World War II]] doing research on reaction kinetics, and then became a member of the Air Ministry Research Establishment, working on [[radar]]. In 1940 he became engaged in operational research at the [[Royal Air Force]] headquarters, holding the honorary rank of Wing Commander R.A.F. He was awarded his PhD after the war in 1949.<ref name=kphd>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=X-ray studies of certain crystalline proteins : the crystal structure of foetal and adult sheep haemoglobins and of horse myoglobin|first= John Cowdery|last=Kendrew|date=1949|url=http://ulmss-newton.lib.cam.ac.uk/vwebv/holdingsInfo?bibId=39466|id={{EThOS|uk.bl.ethos.648050}}|website=lib.cam.ac.uk}}</ref>
Kendrew was born in [[Oxford]], son of [[Wilfrid George Kendrew]], [[reader (academic rank)|reader]] in [[climatology]] in the [[University of Oxford]], and [[Evelyn Sandberg-Vavalà|Evelyn May Graham Sandburg]], art historian. After preparatory school at the [[Dragon School]] in Oxford, he was educated at [[Clifton College]]<ref>"Clifton College Register" Muirhead, J.A.O. p462: Bristol; J.W Arrowsmith for Old Cliftonian Society; April, 1948</ref> in [[Bristol]], 1930–1936. He attended [[Trinity College, Cambridge|Trinity College]], [[University of Cambridge|Cambridge]] in 1936, as a Major Scholar, graduating in chemistry in 1939. He spent the early months of [[World War II]] doing research on reaction kinetics, and then became a member of the Air Ministry Research Establishment, working on [[radar]]. In 1940 he became engaged in operational research at the [[Royal Air Force]] headquarters; commissioned a [[squadron leader]] on 17 September 1941,<ref>{{London Gazette|issue=35301|supp=|page=5793|date=7 October 1941}}</ref> he was appointed an honorary wing commander on 8 June 1944,<ref>{{London Gazette|issue=36633|supp=y|page=3562|date=28 July 1944}}</ref> and relinquished his commission on 5 June 1945.<ref>{{London Gazette|issue=37168|supp=y|page=3552|date=6 July 1945}}</ref> He was awarded his PhD after the war in 1949.<ref name=kphd>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=X-ray studies of certain crystalline proteins : the crystal structure of foetal and adult sheep haemoglobins and of horse myoglobin|first=John Cowdery|last=Kendrew|date=1949|url=http://ulmss-newton.lib.cam.ac.uk/vwebv/holdingsInfo?bibId=39466|id={{EThOS|uk.bl.ethos.648050}}|website=lib.cam.ac.uk|access-date=4 December 2017|archive-date=16 September 2018|archive-url=https://web.archive.org/web/20180916060018/https://ulmss-newton.lib.cam.ac.uk/vwebv/holdingsInfo?bibId=39466|url-status=dead}}</ref>


==Research and career==
==Research and career==
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===Crystallography===
===Crystallography===
In 1945 he approached [[Max Perutz]] in the [[Cavendish Laboratory]] in [[Cambridge]]. [[Joseph Barcroft]], a respiratory physiologist, suggested he might make a comparative protein crystallographic study of adult and fetal sheep [[hemoglobin]], and he started that work.
In 1945 he approached [[Max Perutz]] in the [[Cavendish Laboratory]] in [[Cambridge]]. [[Joseph Barcroft]], a respiratory physiologist, suggested he might make a comparative protein crystallographic study of adult and fetal sheep haemoglobin, and he started that work.


In 1947 he became a Fellow of [[Peterhouse, Cambridge|Peterhouse]]; and the [[Medical Research Council (UK)|Medical Research Council]] (MRC) agreed to create a research unit for the study of the molecular structure of biological systems, under the direction of Sir [[Lawrence Bragg]].{{citation needed|date=August 2017}} In 1954 he became a Reader at the Davy-Faraday Laboratory of the [[Royal Institution]] in [[London]].
In 1947 he became a Fellow of [[Peterhouse, Cambridge|Peterhouse]]; and the [[Medical Research Council (UK)|Medical Research Council]] (MRC) agreed to create a research unit for the study of the molecular structure of biological systems, under the direction of Sir [[Lawrence Bragg]].<ref>{{cite web | url = https://www.nobelprize.org/prizes/chemistry/1962/kendrew/biographical/|title = John C. Kendrew Biographical}}</ref> In 1954 he became a Reader at the Davy-Faraday Laboratory of the [[Royal Institution]] in [[London]].


===Crystal structure of myoglobin===
===Crystal structure of myoglobin===
[[File:KendrewMyoglobin.jpg|thumb|300px|John Kendrew with model of myoglobin in progress. Copyright by the Laboratory of Molecular Biology in Cambridge, England.]]
[[File:KendrewMyoglobin.jpg|thumb|300px|John Kendrew with model of myoglobin in progress. Copyright by the Laboratory of Molecular Biology in Cambridge, England.]]
Kendrew shared the 1962 [[Nobel Prize]] for [[chemistry]] with [[Max Perutz]] for determining the first atomic structures of [[protein]]s using [[X-ray crystallography]]. Their work was done at what is now the [[MRC Laboratory of Molecular Biology]] in [[Cambridge]]. Kendrew determined the structure of the protein [[myoglobin]], which stores oxygen in [[muscle]] [[cell (biology)|cells]]. On Saturday 20 October 1962 the award of Nobel prizes to John Kendrew and Max Perutz, and to Crick, Watson, and Wilkins was satirised in a short sketch in the BBC TV programme [[That Was The Week That Was]] with the Nobel Prizes being referred to as 'The Alfred Nobel Peace Pools'.
Kendrew shared the 1962 [[Nobel Prize]] for [[chemistry]] with [[Max Perutz]] for determining the first atomic structures of [[protein]]s using [[X-ray crystallography]]. Their work was done at what is now the [[MRC Laboratory of Molecular Biology]] in [[Cambridge]]. Kendrew determined the structure of the protein [[myoglobin]], which stores oxygen in [[muscle]] [[cell (biology)|cells]].<ref name="Stoddart">{{cite journal |last1=Stoddart |first1=Charlotte |title=Structural biology: How proteins got their close-up |journal=Knowable Magazine |date=1 March 2022 |doi=10.1146/knowable-022822-1|doi-access=free |url=https://knowablemagazine.org/article/living-world/2022/structural-biology-how-proteins-got-their-closeup |access-date=25 March 2022}}</ref>


In 1947 the MRC agreed to make a research unit for the Study of the Molecular Structure of Biological Systems. The original studies were on the structure of sheep [[hemoglobin]], but when this work had progressed as far as was possible using the resources then available, Kendrew embarked on the study of [[myoglobin]], a molecule only a quarter the size of the hemoglobin molecule. His initial source of raw material was [[horse]] heart, but the crystals thus obtained were too small for X-ray analysis. Kendrew realized that the oxygen-conserving tissue of [[diving mammals]] could offer a better prospect, and a chance encounter led to his acquiring a large chunk of [[whale meat]] from Peru. Whale myoglobin did give large crystals with clean X-ray diffraction patterns. However, the problem still remained insurmountable, until in 1953 [[Max Perutz]] discovered that the [[phase problem]] in analysis of the diffraction patterns could be solved by [[multiple isomorphous replacement]] — comparison of patterns from several crystals; one from the native protein, and others that had been soaked in solutions of heavy metals and had metal ions introduced in different well-defined positions. An electron density map at 6 [[angstrom]] (0.6 [[nanometre]]) resolution was obtained by 1957, and by 1959 an atomic model could be built at 2 angstrom (0.2&nbsp;nm) resolution.<ref>{{cite journal |pmid=18990802 |title=Structure of myoglobin: A three-dimensional Fourier synthesis at 2 A. resolution. | doi=10.1038/185422a0 | volume=185 |date=February 1960 |journal=Nature |pages=422–7 | last1 = Kendrew | first1 = JC | last2 = Dickerson | first2 = RE | last3 = Strandberg | first3 = BE |issue=4711 |display-authors=etal|bibcode=1960Natur.185..422K |s2cid=4167651 }}</ref>
In 1947 the MRC agreed to make a research unit for the Study of the Molecular Structure of Biological Systems. The original studies were on the structure of sheep haemoglobin, but when this work had progressed as far as was possible using the resources then available, Kendrew embarked on the study of [[myoglobin]], a molecule only a quarter the size of the haemoglobin molecule. His initial source of raw material was [[horse]] heart, but the crystals thus obtained were too small for X-ray analysis. Kendrew realized that the oxygen-conserving tissue of [[diving mammals]] could offer a better prospect, and a chance encounter led to his acquiring a large chunk of [[whale meat]] from Peru. Whale myoglobin did give large crystals with clean X-ray diffraction patterns.<ref name="Stoddart"/> However, the problem still remained insurmountable, until in 1953 [[Max Perutz]] discovered that the [[phase problem]] in analysis of the diffraction patterns could be solved by [[multiple isomorphous replacement]] — comparison of patterns from several crystals; one from the native protein, and others that had been soaked in solutions of heavy metals and had metal ions introduced in different well-defined positions. An electron density map at 6 [[angstrom]] (0.6 [[nanometre]]) resolution was obtained by 1957, and by 1959 an atomic model could be built at 2 angstrom (0.2&nbsp;nm) resolution.<ref>{{cite journal |pmid=18990802 |title=Structure of myoglobin: A three-dimensional Fourier synthesis at 2 A. resolution. | doi=10.1038/185422a0 | volume=185 |date=February 1960 |journal=Nature |pages=422–7 | last1 = Kendrew | first1 = JC | last2 = Dickerson | first2 = RE | last3 = Strandberg | first3 = BE |issue=4711 |display-authors=etal|bibcode=1960Natur.185..422K |s2cid=4167651 }}</ref>


===Later career===
===Later career===
In 1963, Kendrew became one of the founders of the [[European Molecular Biology Organization]]; as well, he founded and was for many years editor-in-chief of the [[Journal of Molecular Biology]]. He became Fellow of the American Society of Biological Chemists in 1967 and honorary member of the [[International Academy of Science, Munich]]. In 1974, he succeeded in persuading governments to establish the [[European Molecular Biology Laboratory]] (EMBL) in [[Heidelberg]] and became its first director. He was knighted in 1974.<ref name="frs"/> From 1974 to 1979, he was a Trustee of the [[British Museum]], and from 1974 to 1988 he was successively Secretary General, Vice-President, and President of the [[International Council of Scientific Unions]].
In 1963, Kendrew became one of the founders of the [[European Molecular Biology Organization]]; he also founded the ''[[Journal of Molecular Biology]]'' and was for many years its editor-in-chief. He became Fellow of the American Society of Biological Chemists in 1967 and honorary member of the International Academy of Science, Munich. In 1974, he succeeded in persuading governments to establish the [[European Molecular Biology Laboratory]] (EMBL) in [[Heidelberg]] and became its first director. He was knighted in 1974.<ref name="frs"/> From 1974 to 1979, he was a Trustee of the [[British Museum]], and from 1974 to 1988 he was successively Secretary General, Vice-President, and President of the [[International Council of Scientific Unions]].


After his retirement from EMBL, Kendrew became President of [[St John's College, Oxford|St John's College]] at [[Oxford University]], a post he held from 1981 to 1987. In his will, he designated his bequest to St John's College for studentships in science and in music, for students from developing countries. The ''Kendrew Quadrangle'' at St John's College in Oxford, officially opened on 16 October 2010, is named after him.<ref>{{cite web | url=https://www.sjc.ox.ac.uk/discover/about-college/college-buildings/21st-century/ | title=The 21st Century: Kendrew Quadrangle | publisher=St John's College, Oxford | year=2020 | access-date=2 June 2020}}</ref>
After his retirement from EMBL, Kendrew became President of [[St John's College, Oxford|St John's College]] at the [[University of Oxford]], a post he held from 1981 to 1987. In his will, he designated his bequest to St John's College for studentships in science and in music, for students from developing countries. The ''Kendrew Quadrangle'' at St John's College in Oxford, officially opened on 16 October 2010, is named after him.<ref>{{cite web | url=https://www.sjc.ox.ac.uk/discover/about-college/college-buildings/21st-century/ | title=The 21st Century: Kendrew Quadrangle | publisher=St John's College, Oxford | year=2020 | access-date=2 June 2020}}</ref>


Kendrew was married to the former Elizabeth Jarvie (née Gorvin) from 1948 to 1956. Their marriage ended in divorce. Kendrew was subsequently partners with the artist Ruth Harris.<ref name="frs"/> He left no survivors.<ref>{{cite news | author=Wolfgang Saxon | title=John C. Kendrew Dies at 80; Biochemist Won Nobel in '62 | url=https://www.nytimes.com/1997/08/30/world/john-c-kendrew-dies-at-80-biochemist-won-nobel-in-62.html | work=The New York Times | date=1997-08-30 | access-date=2020-06-02}}</ref>
Kendrew was married to the former Elizabeth Jarvie (née Gorvin) from 1948 to 1956. Their marriage ended in divorce. Kendrew was subsequently partners with the artist Ruth Harris.<ref name="frs"/> He had no surviving children.<ref>{{cite news | author=Wolfgang Saxon | title=John C. Kendrew Dies at 80; Biochemist Won Nobel in '62 | url=https://www.nytimes.com/1997/08/30/world/john-c-kendrew-dies-at-80-biochemist-won-nobel-in-62.html | work=The New York Times | date=1997-08-30 | access-date=2020-06-02}}</ref>


A biography of John Kendrew, titled ''A Place in History: The Biography of John C. Kendrew'', by Paul M. Wassarman was published by Oxford University Press in March 2020.
A biography of Kendrew, entitled ''A Place in History: The Biography of John C. Kendrew'', by [[Paul M. Wassarman]] was published by [[Oxford University Press]] in 2020.


===Selected Publications by Kendrew===
===Selected publications===
{{div col|colwidth=35em}}
{{div col|colwidth=35em}}
*{{cite journal |pmid=18144277 |date=Apr 1949 |last1=Kendrew |first1=JC |title=Foetal haemoglobin |volume=8 |issue=30 |pages=80–5 |issn=0160-9327 |journal=Endeavour}}
*{{cite journal |pmid=18144277 |date=Apr 1949 |last1=Kendrew |first1=JC |title=Foetal haemoglobin |volume=8 |issue=30 |pages=80–5 |issn=0160-9327 |journal=Endeavour}}
*{{cite journal |pmid=13214049 |doi=10.1038/174946a0 |date=Nov 1954 |last1=Kendrew |first1=JC |last2=Parrish |last3=Marrack |last4=Orlans |title=The species specificity of myoglobin |volume=174 |issue=4438 |pages=946–9 |issn=0028-0836 |journal=Nature |first2=RG |first3=JR |first4=ES|bibcode = 1954Natur.174..946K |s2cid=4281674 }}
*{{cite journal |pmid=13214049 |doi=10.1038/174946a0 |date=Nov 1954 |last1=Kendrew |first1=JC |last2=Parrish |last3=Marrack |last4=Orlans |title=The species specificity of myoglobin |volume=174 |issue=4438 |pages=946–9 |issn=0028-0836 |journal=Nature |first2=RG |first3=JR |first4=ES|bibcode = 1954Natur.174..946K |s2cid=4281674 }}
*{{cite journal |pmid=13235845 |doi=10.1038/175206b0 |date=Jan 1955 |last1=Kendrew |first1=JC |last2=Parris |title=Imidazole complexes of myoglobin and the position of the haem group |volume=175 |issue=4448 |pages=206–7 |issn=0028-0836 |journal=Nature |first2=RG|bibcode = 1955Natur.175..206K |s2cid=37160617 }}
*{{cite journal |pmid=13235845 |doi=10.1038/175206b0 |date=Jan 1955 |last1=Kendrew |first1=JC |last2=Parris |title=Imidazole complexes of myoglobin and the position of the haem group |volume=175 |issue=4448 |pages=206–7 |issn=0028-0836 |journal=Nature |first2=RG|bibcode = 1955Natur.175..206K |s2cid=37160617 }}
*{{cite journal |pmid=13369569 |doi=10.1038/178905a0 |date=Oct 1956 |last1=Ingram |first1=DJ |last2=Kendrew |title=Orientation of the haem group in myoglobin and its relation to the polypeptide chain direction |volume=178 |issue=4539 |pages=905–6 |issn=0028-0836 |journal=Nature |first2=JC|bibcode = 1956Natur.178..905I }}
*{{cite journal |pmid=13369569 |doi=10.1038/178905a0 |date=Oct 1956 |last1=Ingram |first1=DJ |last2=Kendrew |title=Orientation of the haem group in myoglobin and its relation to the polypeptide chain direction |volume=178 |issue=4539 |pages=905–6 |issn=0028-0836 |journal=Nature |first2=JC|bibcode = 1956Natur.178..905I |s2cid=26921410 }}
*{{cite journal |pmid=13517261 |doi=10.1038/181662a0 |date=Mar 1958 |last1=Kendrew |first1=JC |last2=Bodo |last3=Dintzis |last4=Parrish |last5=Wyckoff |last6=Phillips |title=A three-dimensional model of the myoglobin molecule obtained by x-ray analysis |volume=181 |issue=4610 |pages=662–6 |issn=0028-0836 |journal=Nature |first2=G |first3=HM |first4=RG |first5=H |first6=DC|bibcode = 1958Natur.181..662K |s2cid=4162786 }}
*{{cite journal |pmid=13517261 |doi=10.1038/181662a0 |date=Mar 1958 |last1=Kendrew |first1=JC |last2=Bodo |last3=Dintzis |last4=Parrish |last5=Wyckoff |last6=Phillips |title=A three-dimensional model of the myoglobin molecule obtained by x-ray analysis |volume=181 |issue=4610 |pages=662–6 |issn=0028-0836 |journal=Nature |first2=G |first3=HM |first4=RG |first5=H |first6=DC|bibcode = 1958Natur.181..662K |s2cid=4162786 }}
*{{cite journal |pmid=13672267 |date=Jul 1959 |last1=Kendrew |first1=JC |title=Structure and function in myoglobin and other proteins |volume=18 |issue=2, Part 1 |pages=740–51 |issn=0014-9446 |journal=Federation Proceedings}}
*{{cite journal |pmid=13672267 |date=Jul 1959 |last1=Kendrew |first1=JC |title=Structure and function in myoglobin and other proteins |volume=18 |issue=2, Part 1 |pages=740–51 |issn=0014-9446 |journal=Federation Proceedings}}
*{{cite journal |pmid=13752474 |doi=10.1038/190666a0 |date=May 1961 |last1=Kendrew |first1=JC |last2=Watson |last3=Strandberg |last4=Dickerson |last5=Phillips |last6=Shore |title=The amino-acid sequence x-ray methods, and its correlation with chemical data |volume=190 |pages=666–70 |issn=0028-0836 |journal=Nature |first2=HC |first3=BE |first4=RE |first5=DC |first6=VC|bibcode = 1961Natur.190..666K |issue=4777|s2cid=39469512 }}
*{{cite journal |pmid=13752474 |doi=10.1038/190666a0 |date=May 1961 |last1=Kendrew |first1=JC |last2=Watson |last3=Strandberg |last4=Dickerson |last5=Phillips |last6=Shore |title=The amino-acid sequence x-ray methods, and its correlation with chemical data |volume=190 |pages=666–70 |issn=0028-0836 |journal=Nature |first2=HC |first3=BE |first4=RE |first5=DC |first6=VC|bibcode = 1961Natur.190..666K |issue=4777|s2cid=39469512 }}
*{{cite journal |pmid=13783432 |doi=10.1038/190670a0 |date=May 1961 |last1=Watson |first1=HC |last2=Kendrew |title=The amino-acid sequence of sperm whale myoglobin. Comparison between the amino-acid sequences of sperm whale myoglobin and of human hemoglobin |volume=190 |pages=670–2 |issn=0028-0836 |journal=Nature |first2=JC|bibcode = 1961Natur.190..670W |issue=4777|s2cid=4170869 }}
*{{cite journal |pmid=13783432 |doi=10.1038/190670a0 |date=May 1961 |last1=Watson |first1=HC |last2=Kendrew |title=The amino-acid sequence of sperm whale myoglobin. Comparison between the amino-acid sequences of sperm whale myoglobin and of human hæmoglobin |volume=190 |pages=670–2 |issn=0028-0836 |journal=Nature |first2=JC|bibcode = 1961Natur.190..670W |issue=4777|s2cid=4170869 }}
*{{cite journal |pmid=14455128 |date=Dec 1961 |last1=Kendrew |first1=JC |title=The three-dimensional structure of a protein molecule |volume=205 |pages=96–110 |issn=0036-8733 | journal=Scientific American | doi=10.1038/scientificamerican1261-96 | issue=6 | bibcode=1961SciAm.205f..96K }}
*{{cite journal |pmid=14455128 |date=Dec 1961 |last1=Kendrew |first1=JC |title=The three-dimensional structure of a protein molecule |volume=205 |pages=96–110 |issn=0036-8733 | journal=Scientific American | doi=10.1038/scientificamerican1261-96 | issue=6 | bibcode=1961SciAm.205f..96K }}
*{{cite journal |pmid=14031911 |doi=10.1016/0010-406X(62)90009-9 |date=Oct 1962 |last1=Kendrew |first1=JC |title=The structure of globular proteins |volume=4 |pages=249–52 |issn=0010-406X |journal=Comparative Biochemistry and Physiology |issue=2–4}}
*{{cite journal |pmid=14031911 |doi=10.1016/0010-406X(62)90009-9 |date=Oct 1962 |last1=Kendrew |first1=JC |title=The structure of globular proteins |volume=4 |pages=249–52 |issn=0010-406X |journal=Comparative Biochemistry and Physiology |issue=2–4}}
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==Further reading==
==Further reading==
* John Finch; 'A Nobel Fellow On Every Floor', Medical Research Council 2008, 381 pp, {{ISBN|978-1-84046-940-0}}; this book is all about the MRC Laboratory of Molecular Biology, Cambridge.
* John Finch; 'A Nobel Fellow on Every Floor', Medical Research Council 2008, 381 pp, {{ISBN|978-1-84046-940-0}}; this book is all about the MRC Laboratory of Molecular Biology, Cambridge.
⚫
* {{Nobelprize|name=John C. Kendrew}}
* [https://global.oup.com/academic/product/a-place-in-history-9780199732043?cc=us&lang=en& Oxford University Press, page on Paul M. Wassarman, ''A Place in History''], {{ISBN|9780199732043}}, 2020
* [https://global.oup.com/academic/product/a-place-in-history-9780199732043?cc=us&lang=en& Oxford University Press, page on Paul M. Wassarman, ''A Place in History''], {{ISBN|9780199732043}}, 2020

==External links==
⚫
* {{Nobelprize|name=John C. Kendrew}}
* {{NPG name}}


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Latest revision as of 05:20, 26 November 2024

For the Industrial Revolution-era designer, see John Kendrew (inventor).

John Kendrew
CBE FRS
Born
John Cowdery Kendrew

(1917-03-24)24 March 1917
Oxford, England
Died23 August 1997(1997-08-23) (aged 80)
Cambridge, England
EducationClifton College, University of Cambridge
Known forHaem-containing proteins
Awards
Scientific career
FieldsCrystallography
InstitutionsMRC Laboratory of Molecular Biology
Peterhouse, Cambridge
Royal Air Force
ThesisX-ray studies of certain crystalline proteins : the crystal structure of foetal and adult sheep haemoglobins and of horse myoglobin (1949)
Academic advisorsMax Perutz
Doctoral students
Other notable studentsJames D. Watson (postdoc)[2]
Military career
Allegiance United Kingdom
Service / branch Royal Air Force
Years of service1941–1945
RankWing Commander (RAFVR)
Battles / warsSecond World War

Sir John Cowdery Kendrew, CBE FRS[3] (24 March 1917 – 23 August 1997) was an English biochemist, crystallographer, and science administrator. Kendrew shared the 1962 Nobel Prize in Chemistry with Max Perutz, for their work at the Cavendish Laboratory to investigate the structure of haem-containing proteins.

Education and early life

[edit]

Kendrew was born in Oxford, son of Wilfrid George Kendrew, reader in climatology in the University of Oxford, and Evelyn May Graham Sandburg, art historian. After preparatory school at the Dragon School in Oxford, he was educated at Clifton College[4] in Bristol, 1930–1936. He attended Trinity College, Cambridge in 1936, as a Major Scholar, graduating in chemistry in 1939. He spent the early months of World War II doing research on reaction kinetics, and then became a member of the Air Ministry Research Establishment, working on radar. In 1940 he became engaged in operational research at the Royal Air Force headquarters; commissioned a squadron leader on 17 September 1941,[5] he was appointed an honorary wing commander on 8 June 1944,[6] and relinquished his commission on 5 June 1945.[7] He was awarded his PhD after the war in 1949.[8]

Research and career

[edit]

During the war years, he became increasingly interested in biochemical problems, and decided to work on the structure of proteins.

Crystallography

[edit]

In 1945 he approached Max Perutz in the Cavendish Laboratory in Cambridge. Joseph Barcroft, a respiratory physiologist, suggested he might make a comparative protein crystallographic study of adult and fetal sheep haemoglobin, and he started that work.

In 1947 he became a Fellow of Peterhouse; and the Medical Research Council (MRC) agreed to create a research unit for the study of the molecular structure of biological systems, under the direction of Sir Lawrence Bragg.[9] In 1954 he became a Reader at the Davy-Faraday Laboratory of the Royal Institution in London.

Crystal structure of myoglobin

[edit]
John Kendrew with model of myoglobin in progress. Copyright by the Laboratory of Molecular Biology in Cambridge, England.

Kendrew shared the 1962 Nobel Prize for chemistry with Max Perutz for determining the first atomic structures of proteins using X-ray crystallography. Their work was done at what is now the MRC Laboratory of Molecular Biology in Cambridge. Kendrew determined the structure of the protein myoglobin, which stores oxygen in muscle cells.[10]

In 1947 the MRC agreed to make a research unit for the Study of the Molecular Structure of Biological Systems. The original studies were on the structure of sheep haemoglobin, but when this work had progressed as far as was possible using the resources then available, Kendrew embarked on the study of myoglobin, a molecule only a quarter the size of the haemoglobin molecule. His initial source of raw material was horse heart, but the crystals thus obtained were too small for X-ray analysis. Kendrew realized that the oxygen-conserving tissue of diving mammals could offer a better prospect, and a chance encounter led to his acquiring a large chunk of whale meat from Peru. Whale myoglobin did give large crystals with clean X-ray diffraction patterns.[10] However, the problem still remained insurmountable, until in 1953 Max Perutz discovered that the phase problem in analysis of the diffraction patterns could be solved by multiple isomorphous replacement — comparison of patterns from several crystals; one from the native protein, and others that had been soaked in solutions of heavy metals and had metal ions introduced in different well-defined positions. An electron density map at 6 angstrom (0.6 nanometre) resolution was obtained by 1957, and by 1959 an atomic model could be built at 2 angstrom (0.2 nm) resolution.[11]

Later career

[edit]

In 1963, Kendrew became one of the founders of the European Molecular Biology Organization; he also founded the Journal of Molecular Biology and was for many years its editor-in-chief. He became Fellow of the American Society of Biological Chemists in 1967 and honorary member of the International Academy of Science, Munich. In 1974, he succeeded in persuading governments to establish the European Molecular Biology Laboratory (EMBL) in Heidelberg and became its first director. He was knighted in 1974.[3] From 1974 to 1979, he was a Trustee of the British Museum, and from 1974 to 1988 he was successively Secretary General, Vice-President, and President of the International Council of Scientific Unions.

After his retirement from EMBL, Kendrew became President of St John's College at the University of Oxford, a post he held from 1981 to 1987. In his will, he designated his bequest to St John's College for studentships in science and in music, for students from developing countries. The Kendrew Quadrangle at St John's College in Oxford, officially opened on 16 October 2010, is named after him.[12]

Kendrew was married to the former Elizabeth Jarvie (née Gorvin) from 1948 to 1956. Their marriage ended in divorce. Kendrew was subsequently partners with the artist Ruth Harris.[3] He had no surviving children.[13]

A biography of Kendrew, entitled A Place in History: The Biography of John C. Kendrew, by Paul M. Wassarman was published by Oxford University Press in 2020.

Selected publications

[edit]
  • Kendrew, JC (April 1949). "Foetal haemoglobin". Endeavour. 8 (30): 80–5. ISSN 0160-9327. PMID 18144277.
  • Kendrew, JC; Parrish, RG; Marrack, JR; Orlans, ES (November 1954). "The species specificity of myoglobin". Nature. 174 (4438): 946–9. Bibcode:1954Natur.174..946K. doi:10.1038/174946a0. ISSN 0028-0836. PMID 13214049. S2CID 4281674.
  • Kendrew, JC; Parris, RG (January 1955). "Imidazole complexes of myoglobin and the position of the haem group". Nature. 175 (4448): 206–7. Bibcode:1955Natur.175..206K. doi:10.1038/175206b0. ISSN 0028-0836. PMID 13235845. S2CID 37160617.
  • Ingram, DJ; Kendrew, JC (October 1956). "Orientation of the haem group in myoglobin and its relation to the polypeptide chain direction". Nature. 178 (4539): 905–6. Bibcode:1956Natur.178..905I. doi:10.1038/178905a0. ISSN 0028-0836. PMID 13369569. S2CID 26921410.
  • Kendrew, JC; Bodo, G; Dintzis, HM; Parrish, RG; Wyckoff, H; Phillips, DC (March 1958). "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis". Nature. 181 (4610): 662–6. Bibcode:1958Natur.181..662K. doi:10.1038/181662a0. ISSN 0028-0836. PMID 13517261. S2CID 4162786.
  • Kendrew, JC (July 1959). "Structure and function in myoglobin and other proteins". Federation Proceedings. 18 (2, Part 1): 740–51. ISSN 0014-9446. PMID 13672267.
  • Kendrew, JC; Watson, HC; Strandberg, BE; Dickerson, RE; Phillips, DC; Shore, VC (May 1961). "The amino-acid sequence x-ray methods, and its correlation with chemical data". Nature. 190 (4777): 666–70. Bibcode:1961Natur.190..666K. doi:10.1038/190666a0. ISSN 0028-0836. PMID 13752474. S2CID 39469512.
  • Watson, HC; Kendrew, JC (May 1961). "The amino-acid sequence of sperm whale myoglobin. Comparison between the amino-acid sequences of sperm whale myoglobin and of human hæmoglobin". Nature. 190 (4777): 670–2. Bibcode:1961Natur.190..670W. doi:10.1038/190670a0. ISSN 0028-0836. PMID 13783432. S2CID 4170869.
  • Kendrew, JC (December 1961). "The three-dimensional structure of a protein molecule". Scientific American. 205 (6): 96–110. Bibcode:1961SciAm.205f..96K. doi:10.1038/scientificamerican1261-96. ISSN 0036-8733. PMID 14455128.
  • Kendrew, JC (October 1962). "The structure of globular proteins". Comparative Biochemistry and Physiology. 4 (2–4): 249–52. doi:10.1016/0010-406X(62)90009-9. ISSN 0010-406X. PMID 14031911.
  • Kendrew, John C. (1966). The thread of life: an introduction to molecular biology. London: Bell & Hyman. ISBN 978-0-7135-0618-1.

References

[edit]
  1. ^ Huxley, Hugh Esmor (1953). Investigations of biological structures by X-ray methods : the structure of muscle. lib.cam.ac.uk (PhD thesis). University of Cambridge. OCLC 885437514. EThOS uk.bl.ethos.604904. Archived from the original on 19 May 2022. Retrieved 4 December 2017.
  2. ^ a b c "John Kendrew academic genealogy". academictree.org.
  3. ^ a b c Holmes, K. C. (2001). "Sir John Cowdery Kendrew. 24 March 1917 - 23 August 1997: Elected F.R.S. 1960". Biographical Memoirs of Fellows of the Royal Society. 47: 311–332. doi:10.1098/rsbm.2001.0018. hdl:11858/00-001M-0000-0028-EC77-7. PMID 15124647.
  4. ^ "Clifton College Register" Muirhead, J.A.O. p462: Bristol; J.W Arrowsmith for Old Cliftonian Society; April, 1948
  5. ^ "No. 35301". The London Gazette. 7 October 1941. p. 5793.
  6. ^ "No. 36633". The London Gazette (Supplement). 28 July 1944. p. 3562.
  7. ^ "No. 37168". The London Gazette (Supplement). 6 July 1945. p. 3552.
  8. ^ Kendrew, John Cowdery (1949). X-ray studies of certain crystalline proteins : the crystal structure of foetal and adult sheep haemoglobins and of horse myoglobin. lib.cam.ac.uk (PhD thesis). University of Cambridge. EThOS uk.bl.ethos.648050. Archived from the original on 16 September 2018. Retrieved 4 December 2017.
  9. ^ "John C. Kendrew Biographical".
  10. ^ a b Stoddart, Charlotte (1 March 2022). "Structural biology: How proteins got their close-up". Knowable Magazine. doi:10.1146/knowable-022822-1. Retrieved 25 March 2022.
  11. ^ Kendrew, JC; Dickerson, RE; Strandberg, BE; et al. (February 1960). "Structure of myoglobin: A three-dimensional Fourier synthesis at 2 A. resolution". Nature. 185 (4711): 422–7. Bibcode:1960Natur.185..422K. doi:10.1038/185422a0. PMID 18990802. S2CID 4167651.
  12. ^ "The 21st Century: Kendrew Quadrangle". St John's College, Oxford. 2020. Retrieved 2 June 2020.
  13. ^ Wolfgang Saxon (30 August 1997). "John C. Kendrew Dies at 80; Biochemist Won Nobel in '62". The New York Times. Retrieved 2 June 2020.

Further reading

[edit]
[edit]
Academic offices
Preceded by President of St John's College, Oxford
1981–1987 		Succeeded by
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