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Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.Statistical mechanics applied to cooperative ligand binding to proteins.Interaction of hemoglobin with three ligans: organic phosphates and the Bohr effect.Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas.Linearity of the hemoglobin oxidation bohr effectThe three-state model: a minimal allosteric description of homotropic and heterotropic effects in the binding of ligands to hemoglobin.The interaction of inositol hexaphosphate with methaemoglobin.Fourth gaddum memorial lecture, school of pharmacy, university of london, january 1973.Triphosphate spin-label studies of allosteric interactions in hemoglobin.High-resolution proton NMR studies of low affinity hemoglobins.
P2860
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P2860
description
1972 nî lūn-bûn
@nan
1972年の論文
@ja
1972年学术文章
@wuu
1972年学术文章
@zh
1972年学术文章
@zh-cn
1972年学术文章
@zh-hans
1972年学术文章
@zh-my
1972年学术文章
@zh-sg
1972年學術文章
@yue
1972年學術文章
@zh-hant
name
States of hemoglobin in solution.
@en
States of hemoglobin in solution.
@nl
type
label
States of hemoglobin in solution.
@en
States of hemoglobin in solution.
@nl
prefLabel
States of hemoglobin in solution.
@en
States of hemoglobin in solution.
@nl
P356
P1433
P1476
States of hemoglobin in solution.
@en
P2093
McConnell HM
P304
P356
10.1021/BI00775A024
P407
P577
1972-12-01T00:00:00Z