Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Francine R. Smith"'
Autor:
Donald W. Pettigrew, Benjamin W. Turner, Winston F. Moo-Penn, Francine R. Smith, Bo E. Hedlund, Michael L. Doyle, George J. Turner, Gary K. Ackers, Frederic Galacteros, Donald L. Rucknagel
Publikováno v:
Proteins: Structure, Function, and Genetics. 14:333-350
Free energies of oxygen-linked subunit assembly and cooperative interaction have been determined for 34 molecular species of human hemoglobin, which differ by amino acid alterations as a result of mutation or chemical modification at specific sites.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ba74402946ce43d9bda8bf5ead925ab
https://doi.org/10.1002/prot.340140303
https://doi.org/10.1002/prot.340140303
Publikováno v:
Proteins: Structure, Function, and Genetics. 10:81-91
Carbonmonoxy hemoglobin Ypsilanti (beta 99 Asp-Tyr) exhibits a quaternary form distinctly different from any structures previously observed for human hemoglobins. The relative orientation of alpha beta dimers in the new quaternary form lies well outs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9093fa0f3b7acfad9d36a8d4894bee4a
https://doi.org/10.1002/prot.340100202
https://doi.org/10.1002/prot.340100202
Publikováno v:
The Journal of biological chemistry. 272(9)
The assembly of Scapharca dimeric hemoglobin as a function of ligation has been explored by analytical gel chromatography, sedimentation equilibrium, and oxygen binding experiments to test the proposal that its cooperativity is based on quaternary en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad16792f7d45ab8c2bcc17e804be67ce
https://pubmed.ncbi.nlm.nih.gov/9038179
https://pubmed.ncbi.nlm.nih.gov/9038179
Publikováno v:
Proteins. 18(3)
Cyanomet human hemoglobin has been crystallized at a chloride ion concentration and pH similar to physiological conditions. Molecular replacement calculations definitively show that the hemoglobin subunits are arranged in the Y quaternary form recent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1abed534b3de13247e6d12344531083b
https://pubmed.ncbi.nlm.nih.gov/8202470
https://pubmed.ncbi.nlm.nih.gov/8202470
Publikováno v:
Proceedings of the National Academy of Sciences. 84:7089-7093
In a previous study on cyanomethemoglobin the 10 tetrameric species (each with a unique combination of ligated and unligated subunits) were found to exhibit three distinct free energies of cooperative interaction. The distribution of these free energ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::236bc20531df52c70ebaabf901bca2b6
https://doi.org/10.1073/pnas.84.20.7089
https://doi.org/10.1073/pnas.84.20.7089
Autor:
Gary K. Ackers, Francine R. Smith
Publikováno v:
Annual Review of Biophysics and Biophysical Chemistry. 16:583-609
CONTENTS PERSPECTIVES AND OVERVIEW ......•• •........••• 583 DEFINITIONS AND BACKGROUND 586 Hemoglobin Structure and Function. .. . ...... . . . . ....... . . . . . . . . . . . . . . . . . . . . . . ..... . . . . . . . .. .. . . 587 Energ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::643980c608eaf2d4998420fe32373b2a
https://doi.org/10.1146/annurev.bb.16.060187.003055
https://doi.org/10.1146/annurev.bb.16.060187.003055
Publikováno v:
Journal of Molecular Biology. 170:223-242
Individual-site binding curves such as those obtainable from techniques of DNase footprinting or nuclear magnetic resonance spectroscopy can be used to monitor structurally localized events within biopolymers. This paper discusses thermodynamic aspec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d399c42207099896e230a23bd95d53a
https://doi.org/10.1016/s0022-2836(83)80234-4
https://doi.org/10.1016/s0022-2836(83)80234-4
Autor:
Gary K. Ackers, Francine R. Smith
Publikováno v:
Biophysical Journal. 49(1):155-165
Site-specific structural modification is a powerful tool for studying functional mechanisms in proteins where the structures may be manipulated by direct chemical modification, by selection of naturally-occurring mutants, or by site-directed mutagene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25bfb73c55978ecb5945ae4ccf96facd
Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin
Autor:
Francine R. Smith, Gary K. Ackers
Publikováno v:
Proceedings of the National Academy of Sciences. 82:5347-5351
Tetrameric human hemoglobin can assume ten molecular forms that differ in the number and configuration of ligands bound at the four heme sites. For each of these species we have determined the cooperative free energy--i.e., the deviation in free ener
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::115773ba0d03dd60fe5f0a9d9ef31e3c
https://doi.org/10.1073/pnas.82.16.5347
https://doi.org/10.1073/pnas.82.16.5347