Time-resolved x-ray crystallography of heme proteins. - Wikidata - wikimedia - TriplyDB

Time-resolved x-ray crystallography of heme proteins.

Time-resolved x-ray crystallography of heme proteins.

http://www.wikidata.org/entity/Q33330538

about

Nanosecond time-resolved polarization spectroscopies: tools for probing protein reaction mechanisms.Implementing electrostatic polarization cannot fill the gap between experimental and theoretical measurements for the ultrafast fluorescence decay of myoglobin.Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy.Alteration of the α1β2/α2β1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice.Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam Probing early events in ferrous cytochrome c folding with time-resolved natural and magnetic circular dichroism spectroscopies Biophysical characterization of the interaction of human albumin with an anionic porphyrin

P2860

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P2860

Time-resolved x-ray crystallography of heme proteins.

http://www.wikidata.org/entity/Q33330538

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Time-resolved x-ray crystallography of heme proteins.

@ast

Time-resolved x-ray crystallography of heme proteins.

@en

Time-resolved x-ray crystallography of heme proteins.

@nl

type

label

Time-resolved x-ray crystallography of heme proteins.

@ast

Time-resolved x-ray crystallography of heme proteins.

@en

Time-resolved x-ray crystallography of heme proteins.

@nl

prefLabel

Time-resolved x-ray crystallography of heme proteins.

@ast

Time-resolved x-ray crystallography of heme proteins.

@en

Time-resolved x-ray crystallography of heme proteins.

@nl

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S0076-6879(07)37019-5

P1433

Methods in Enzymology

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Time-resolved x-ray crystallography of heme proteins.

@en

P2093

Vukica Srajer

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

William E Royer

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

P2860

Restricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity

Ligand-linked structural transitions in crystals of a cooperative dimeric hemoglobin

Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography

Mutational destabilization of the critical interface water cluster in Scapharca dimeric hemoglobin: structural basis for altered allosteric activity

Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin

Towards automated Laue data processing: application to the choice of optimal X-ray spectrum.

Application of singular value decomposition to the analysis of time-resolved macromolecular x-ray data

New processing tools for weak and/or spatially overlapped macromolecular diffraction patterns.

Immobilization of Scapharca HbI crystals improves data quality in time-resolved crystallographic experiments.

Protein kinetics: structures of intermediates and reaction mechanism from time-resolved x-ray data.

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379-395

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scholarly article

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10.1016/S0076-6879(07)37019-5

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437

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2008-01-01T00:00:00Z

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5418537

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18433638

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3287071

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