A fluctuating quantum model of the CO vibration in carboxyhemoglobin. - Wikidata - awgldk - TriplyDB

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

http://www.wikidata.org/entity/Q33929468

about

Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site.Vibrational ladder climbing in carboxy-hemoglobin: effects of the protein environment.Mixed quantum-classical simulations of the vibrational relaxation of photolyzed carbon monoxide in a hemoprotein.

P2860

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P2860

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

http://www.wikidata.org/entity/Q33929468

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

@ast

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

@en

type

label

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

@ast

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

@en

prefLabel

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

@ast

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

@en

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P1433

Journal of Chemical Physics

P1476

A fluctuating quantum model of the CO vibration in carboxyhemoglobin.

@en

P2093

Christoph Meier

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

Cyril Falvo

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

P2860

Crystal structures of myoglobin-ligand complexes at near-atomic resolution.

All-atom empirical potential for molecular modeling and dynamics studies of proteins

Influence of the heme pocket conformation on the structure and vibrations of the Fe-CO bond in myoglobin: a QM/MM density functional study.

The influence of aqueous versus glassy solvents on protein dynamics: vibrational echo experiments and molecular dynamics simulations.

Conformational substates and motions in myoglobin. External influences on structure and dynamics.

Infrared characterization of nitric oxide bonding to bovine heart cytochrome c oxidase and myoglobin.

Protein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes.

Polarization shaping in the mid-IR and polarization-based balanced heterodyne detection with application to 2D IR spectroscopy.

Direct observation of fast protein conformational switching

Laser control of chemical reactions

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214106

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scholarly article

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10.1063/1.3592707

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P433

21

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134

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2011-06-01T00:00:00Z

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21663343

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