Zobrazeno 1 - 10 of 54 pro vyhledávání: '"M. Perutz"'
1
Male three-spined sticklebacksGasterosteus aculeatusmake antibiotic nests: a novel form of parental protection?
Autor: T. J. Little, C. Crossan, Victoria A. Braithwaite, M. Palmer, M. Perutz
Publikováno v: Journal of Fish Biology. 73:2380-2389
The egg nest of male three-spined sticklebacks Gasterosteus aculeatus is constructed with a gluelike secretion that this study demonstrates has antimicrobial properties. Glue collected from reproductively active males decreased the growth rate of bac
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d9cab9263d35b840152553c5b13e3841
https://doi.org/10.1111/j.1095-8649.2008.02086.x
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3
Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66—-Thr) and its isolated beta chains
Autor: D. T.-B. Shih, G. Fermi, Celia Bonaventura, Joseph Bonaventura, M. Perutz, Robert Cashon
Publikováno v: Journal of Biological Chemistry. 266:23033-23040
Hemoglobin (Hb) Chico (Lys beta 66----Thr at E10) has a diminished oxygen affinity (Shih, D. T.-b., Jones, R. T., Shih, M. F.-C., Jones, M. B., Koler, R. D., and Howard, J. (1987) Hemoglobin 11, 453-464). Our studies show that its P50 is about twice
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ef377d4c6069ab0374ebdc19d36b895e
https://doi.org/10.1016/s0021-9258(18)54459-8
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4
Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobins
Autor: Z, Derewenda, G, Dodson, P, Emsley, D, Harris, K, Nagai, M, Perutz, J P, Renaud, J P, Reynaud
Publikováno v: Journal of Molecular Biology. 211:515-519
The structures of carbonmonoxyhaemoglobins A and Cowtown (His146 beta----Leu) have been refined at 2.2 A (1 A = 0.1 nm) and 2.3 A resolution, respectively. The least squares fit to the Fe-C-O line makes an angle to the haem normal of about 6 degrees.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c95ca470377f80c777edf437ca7fc43
https://doi.org/10.1016/0022-2836(90)90262-k
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6
Polar zipper sequence in the high-affinity hemoglobin of Ascaris suum: amino acid sequence and structural interpretation
Autor: L Liu, J. Richelle, J. Finch, C. Gielens, M. Perutz, C Trotman, Mark Gerstein, I De Baere, Luc Moens, J Van Beeumen
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 89(10)
The extracellular hemoglobin of Ascaris has an extremely high oxygen affinity (P50 = 0.004 mmHg). It consists of eight identical subunits of molecular weight 40,600. Their sequence, determined by protein chemistry, shows two tandemly linked globin-li
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df6566099898fa12aa1744da73892367
https://pubmed.ncbi.nlm.nih.gov/1584800
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7
Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66----Thr) and its isolated beta chains
Autor: C, Bonaventura, R, Cashon, J, Bonaventura, M, Perutz, G, Fermi, D T, Shih
Publikováno v: The Journal of biological chemistry. 266(34)
Hemoglobin (Hb) Chico (Lys beta 66----Thr at E10) has a diminished oxygen affinity (Shih, D. T.-b., Jones, R. T., Shih, M. F.-C., Jones, M. B., Koler, R. D., and Howard, J. (1987) Hemoglobin 11, 453-464). Our studies show that its P50 is about twice
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2db643acf2448c9562ea2c2535f748de
https://pubmed.ncbi.nlm.nih.gov/1744099
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