The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids
about
Confirmation of a unique intra-dimer cooperativity in the human hemoglobin alpha(1)beta(1)half-oxygenated intermediate supports the symmetry rule model of allosteric regulation.Allosteric effectors influence the tetramer stability of both R- and T-states of hemoglobin A.Disentangling the web of allosteric communication in a homotetramer: heterotropic inhibition in phosphofructokinase from Escherichia coliEntropy-driven intermediate steps of oxygenation may regulate the allosteric behavior of hemoglobinAllosteric effectors do not alter the oxygen affinity of hemoglobin crystals.
P2860
The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The oxygen-binding intermediat ...... using zinc-containing hybrids
@ast
The oxygen-binding intermediat ...... using zinc-containing hybrids
@en
The oxygen-binding intermediat ...... using zinc-containing hybrids
@nl
type
label
The oxygen-binding intermediat ...... using zinc-containing hybrids
@ast
The oxygen-binding intermediat ...... using zinc-containing hybrids
@en
The oxygen-binding intermediat ...... using zinc-containing hybrids
@nl
prefLabel
The oxygen-binding intermediat ...... using zinc-containing hybrids
@ast
The oxygen-binding intermediat ...... using zinc-containing hybrids
@en
The oxygen-binding intermediat ...... using zinc-containing hybrids
@nl
P2093
P2860
P1433
P1476
The oxygen-binding intermediat ...... using zinc-containing hybrids
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(96)79408-0
P407
P577
1996-10-01T00:00:00Z