Zobrazeno 1 - 10
of 116
pro vyhledávání: '"M. F. Perutz"'
Autor:
M F, PERUTZ
Publikováno v:
The Australian journal of science. 8
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3117dcfc44847bf2e4a687d25f4b5e2d
https://pubmed.ncbi.nlm.nih.gov/21026692
https://pubmed.ncbi.nlm.nih.gov/21026692
Autor:
D. Eisenberg, M. F. Perutz, A. D. Buckingham, L. Graf, J. Thornton, D. M. Blow, A. R. Fersht, M. Karplus, L. N. Johnson, F. Rippmann, G. G. Dodson, P. N. Edwards, P. Halling, K. Wüthrich, M. C. R. Symons, K. Marshall, B. L. Vallee, M. Rossi, D. S. Auld, E. Pombo-Villar, M. L. Sinnott, H. B. F. Dixon, A. Berry, D. R. Brown, J. A. Littlechild, A. Thomson, N. Ito, P. F. Knowles, S. S. Taylor, G. E. Schulz, O. Misset
Publikováno v:
Faraday Discuss.. 93:107-129
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db51839b68495e8d876cb9364d7c01b3
https://doi.org/10.1039/fd9929300107
https://doi.org/10.1039/fd9929300107
Autor:
M. F. Perutz
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 46:633-643
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a37399946999a5c9ae6df06f48a066f
https://doi.org/10.1107/s010876739000410x
https://doi.org/10.1107/s010876739000410x
Publikováno v:
Journal of Biological Chemistry. 265:126-132
In Hb Warsaw Val replaces the Phe normally present at the heme contact position beta 42 (CD1). This variant is unstable, and it readily undergoes methemoglobin formation. In DEAE-cellulose chromatography, the variant hemoglobin co-eluted with Hb A; a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::53914de88cf4ddc03ff6811fca2174c3
https://doi.org/10.1016/s0021-9258(19)40204-4
https://doi.org/10.1016/s0021-9258(19)40204-4
Publikováno v:
Journal of molecular biology. 281(4)
The T-structure of human haemoglobin is linked by salt-bridges between its four subunits, formed by the C-terminal arginine residues of the alpha-subunits and the C-terminal histidine residues of the beta-subunits. In the R-structure, these salt-brid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e5813cd456aadd1d4de4c2fa16126d5a
https://pubmed.ncbi.nlm.nih.gov/9710531
https://pubmed.ncbi.nlm.nih.gov/9710531
Autor:
M F, Perutz
Publikováno v:
Molecular medicine (Cambridge, Mass.). 2(6)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::59e7d873e483efdbee8758aa38322d3e
https://pubmed.ncbi.nlm.nih.gov/8972480
https://pubmed.ncbi.nlm.nih.gov/8972480
Autor:
M F, Perutz
Publikováno v:
KOS. (133)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::447f36b100fc9332a3f104cbc2bd69fe
https://pubmed.ncbi.nlm.nih.gov/11636391
https://pubmed.ncbi.nlm.nih.gov/11636391
Publikováno v:
Journal of molecular biology. 239(4)
Chloride reduces the oxygen affinity of mammalian haemoglobin by acting as an allosteric effector that stabilizes the quaternary deoxy (T) structure. Perutz and others showed evidence that it does so by neutralizing electrostatic repulsion by an exce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7ef31d23fb1cdfebdcd3c0ba58c01f71
https://pubmed.ncbi.nlm.nih.gov/8006967
https://pubmed.ncbi.nlm.nih.gov/8006967