Direct observation of photolysis-induced tertiary structural changes in hemoglobin - Wikidata - awgldk - TriplyDB

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

http://www.wikidata.org/entity/Q27641341

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Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix Reverse engineering the cooperative machinery of human hemoglobin Reaction trajectory revealed by a joint analysis of protein data bank Visualizing breathing motion of internal cavities in concert with ligand migration in myoglobin.Discrimination between CO and O 2 in Heme Oxygenase: Comparison of Static Structures and Dynamic Conformation Changes following CO Photolysis Kappa-alpha plot derived structural alphabet and BLOSUM-like substitution matrix for rapid search of protein structure database.Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin A high-throughput screen for porphyrin metal chelatases: application to the directed evolution of ferrochelatases for metalloporphyrin biosynthesis.Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallography Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi.Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100 ps to 10 ms with pump-probe X-ray solution scattering.A quantum-chemical picture of hemoglobin affinity Alteration of the α1β2/α2β1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice.Molecular dynamics simulations of hemoglobin A in different states and bound to DPG: effector-linked perturbation of tertiary conformations and HbA concerted dynamics Cooperative protein structural dynamics of homodimeric hemoglobin linked to water cluster at subunit interface revealed by time-resolved X-ray solution scattering.Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway.An atomistic view on human hemoglobin carbon monoxide migration processes.Coarse-grained and all-atom modeling of structural states and transitions in hemoglobin.

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P2860

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

http://www.wikidata.org/entity/Q27641341

description

2003 nî lūn-bûn

@nan

2003 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հունիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

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2003年論文

@zh-tw

2003年论文

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name

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@ast

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@en

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@nl

type

label

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@ast

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@en

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@nl

prefLabel

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@ast

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@en

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@nl

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PNAS.1230629100

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Direct observation of photolysis-induced tertiary structural changes in hemoglobin

@en

P2093

Jeremy R H Tame

http://www.w3.org/2001/XMLSchema#string

Sam-Yong Park

http://www.w3.org/2001/XMLSchema#string

Yoshitsugu Shiro

http://www.w3.org/2001/XMLSchema#string

P2860

X-ray crystal structure determination and refinement at 1.9 A resolution of isolectin I from the seeds of Lathyrus ochrus

Structure of human oxyhaemoglobin at 2.1 A resolution

The crystal structure of human deoxyhaemoglobin at 1.74 A resolution

Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K

Crystal structure of photolysed carbonmonoxy-myoglobin

The crystal structure of horse deoxyhaemoglobin trapped in the high-affinity (R) state

The CCP4 suite: programs for protein crystallography

Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A.

A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin.

Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction.

P304

7039-7044

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scholarly article

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10.1073/PNAS.1230629100

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12

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100

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Naoya Shibayama

Shin-ichi Adachi

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2003-05-28T00:00:00Z

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10736391

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12773618

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165826

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