The effect of heme on the conformational stability of micro-myoglobin.

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Kinetic intermediates of holo- and apo-myoglobin studied using HDX-TIMS-MS and molecular dynamic simulations.In silico Evaluation of Crosslinking Effects on Denaturant m(eq) values and ΔCp upon Protein Unfolding

P2860

Q35471834-1A6A57B4-011D-47E1-BCA8-A5A18802AD47 Q36571436-F7444C6F-FDA6-442C-B75B-864AFAC558F3

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The effect of heme on the conformational stability of micro-myoglobin.

Item

http://www.wikidata.org/entity/Q50856370

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2007 nî lūn-bûn

@nan

2007年の論文

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2007年学术文章

@wuu

2007年学术文章

@zh

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

@zh-hant

name

The effect of heme on the conformational stability of micro-myoglobin.

@en

The effect of heme on the conformational stability of micro-myoglobin.

@nl

type

Item

label

The effect of heme on the conformational stability of micro-myoglobin.

@en

The effect of heme on the conformational stability of micro-myoglobin.

@nl

prefLabel

The effect of heme on the conformational stability of micro-myoglobin.

@en

The effect of heme on the conformational stability of micro-myoglobin.

@nl

P1476

The effect of heme on the conformational stability of micro-myoglobin.

@en

P2093

Hong-Fang Ji

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

Liang Shen

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

Norbert Müller

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

Rita Grandori

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

P2860

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

Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints

Correlation of DNA exonic regions with protein structural units in haemoglobin

Protein structure, stability and solubility in water and other solvents.

Hydration of denatured and molten globule proteins.

Molecular dynamics studies on the HIV-1 integrase catalytic domain.

Relationship between ion pair geometries and electrostatic strengths in proteins.

To charge or not to charge?

Molecular dynamics simulations of biomolecules.

Role of the conserved NPxxY(x)5,6F motif in the rhodopsin ground state and during activation.

P304

89-96

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P31

scholarly article

P356

10.1111/J.1742-4658.2007.06176.X

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P407

English

P433

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

P478

275

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P577

2007-11-26T00:00:00Z

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

P698

18039332

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

The effect of heme on the conformational stability of micro-myoglobin.

about

P2860

P2860

The effect of heme on the conformational stability of micro-myoglobin.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698