Tryptophan conformations associated with partial unfolding in ribonuclease T1

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The Periplasmic Chaperone Network of Campylobacter jejuni: Evidence that SalC (Cj1289) and PpiD (Cj0694) Are Involved in Maintaining Outer Membrane Integrity.

P2860

Q37723502-22749865-EBC0-4577-879A-80C827A1CC3C

P2860

Tryptophan conformations associated with partial unfolding in ribonuclease T1

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http://www.wikidata.org/entity/Q42563238

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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

Tryptophan conformations associated with partial unfolding in ribonuclease T1

@en

Tryptophan conformations associated with partial unfolding in ribonuclease T1

@nl

type

Item

label

Tryptophan conformations associated with partial unfolding in ribonuclease T1

@en

Tryptophan conformations associated with partial unfolding in ribonuclease T1

@nl

prefLabel

Tryptophan conformations associated with partial unfolding in ribonuclease T1

@en

Tryptophan conformations associated with partial unfolding in ribonuclease T1

@nl

P1476

Tryptophan conformations associated with partial unfolding in ribonuclease T1

@en

P2093

Abel Jonckheer

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

Arnout Ceulemans

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

Samuel L C Moors

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

P2860

Protein folding funnels: a kinetic approach to the sequence-structure relationship

Conformational stability of ribonuclease T1 determined by hydrogen-deuterium exchange

Determination of the NMR structure of Gln25-ribonuclease T1

Crystal structure of RNase T1 complexed with the product nucleotide 3'-GMP. Structural evidence for direct interaction of histidine 40 and glutamic acid 58 with the 2'-hydroxyl group of the ribose

Limits of NMR structure determination using variable target function calculations: ribonuclease T1, a case study

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

On the involvement of electron transfer reactions in the fluorescence decay kinetics heterogeneity of proteins

Conformation heterogeneity in proteins as an origin of heterogeneous fluorescence decays, illustrated by native and denatured ribonuclease T1.

On spectral relaxation in proteins.

The dead-end elimination method, tryptophan rotamers, and fluorescence lifetimes.

P304

1778-1786

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

P31

scholarly article

P356

10.1016/J.BPJ.2009.07.015

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

P407

English

P433

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

P478

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

P50

Yves Engelborghs

Marc De Maeyer

P577

2009-09-01T00:00:00Z

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

P5875

26809707

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

P698

19751684

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

P932

2749795

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

Tryptophan conformations associated with partial unfolding in ribonuclease T1

about

P2860

P2860

Tryptophan conformations associated with partial unfolding in ribonuclease T1

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932