A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin.
about
Reverse engineering the cooperative machinery of human hemoglobinTrans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletionCrystalline ligand transitions in lamprey hemoglobin. Structural evidence for the regulation of oxygen affinityAzide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediatesDirect observation of photolysis-induced tertiary structural changes in hemoglobinQuantitative vibrational dynamics of iron in carbonyl porphyrinsRecruitment of rare 3-grams at functional sites: is this a mechanism for increasing enzyme specificity?Phthalide Derivatives from Angelica Sinensis Decrease Hemoglobin Oxygen Affinity: A New Allosteric-Modulating Mechanism and Potential Use as 2,3-BPG Functional SubstitutesNuclear resonance vibrational spectra of five-coordinate imidazole-ligated iron(II) porphyrinates.New look at hemoglobin allostery.Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.Neuronal hemoglobin affects dopaminergic cells' response to stressContact rearrangements form coupled networks from local motions in allosteric proteins.1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin.The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme.Structure-function relationships in the hammerhead ribozyme probed by base rescue.Electron paramagnetic resonance and oxygen binding studies of alpha-Nitrosyl hemoglobin. A novel oxygen carrier having no-assisted allosteric functions.Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen.Heme Orientation of Cavity Mutant Hemoglobins (His F8 → Gly) in Either α or β Subunits: Circular Dichroism, (1) H NMR, and Resonance Raman Studies.
P2860
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P2860
A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
A test of the role of the prox ...... cooperativity in haemoglobin.
@ast
A test of the role of the prox ...... cooperativity in haemoglobin.
@en
type
label
A test of the role of the prox ...... cooperativity in haemoglobin.
@ast
A test of the role of the prox ...... cooperativity in haemoglobin.
@en
prefLabel
A test of the role of the prox ...... cooperativity in haemoglobin.
@ast
A test of the role of the prox ...... cooperativity in haemoglobin.
@en
P2093
P2860
P356
P1476
A test of the role of the prox ...... cooperativity in haemoglobin.
@en
P2093
P2860
P356
10.1038/NSB0197-78
P577
1997-01-01T00:00:00Z