Compressing the free energy range of substructure stabilities in iso-1-cytochrome c. - Wikidata - awgldk - TriplyDB

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

http://www.wikidata.org/entity/Q42623250

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Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity.The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c Structural transformations of cytochrome c upon interaction with cardiolipin Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability Effect of an Ala81His mutation on the Met80 loop dynamics of iso-1-cytochrome c.Conformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c.Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination.Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.Dynamics of the His79-heme alkaline transition of yeast iso-1-cytochrome c probed by conformationally gated electron transfer with Co(II)bis(terpyridine).Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Ligation and Reactivity of Methionine-Oxidized Cytochrome c.The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c

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P2860

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

http://www.wikidata.org/entity/Q42623250

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

@en

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

@nl

type

label

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

@en

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

@nl

prefLabel

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

@en

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

@nl

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Protein Science

P1476

Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.

@en

P2093

Bruce E Bowler

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

Michael D Williams

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

Michael G Duncan

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

P2860

Oxidation state-dependent conformational changes in cytochrome c

Cooperative omega loops in cytochrome c: role in folding and function

Protein folding and misfolding

Proteinase K from Tritirachium album Limber

Mutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome c

Functional role of a protein foldon--an Omega-loop foldon controls the alkaline transition in ferricytochrome c

Hydrogen exchange behavior of [U-15N]-labeled oxidized and reduced iso-1-cytochrome c.

Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c.

Probing protein structure by limited proteolysis.

Future directions in folding: the multi-state nature of protein structure.

P304

1155-1164

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

P31

scholarly article

P356

10.1002/PRO.120

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

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6

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18

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2009-06-01T00:00:00Z

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26243716

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19472325

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2774426

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