Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

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Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Local and global anatomy of antibody-protein antigen recognition.

P2860

Q47214435-E16ED717-4E74-485F-BAA8-05DABE5528A3 Q47316363-9DC69E5C-177A-4462-9066-B1F5E9605455

P2860

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

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http://www.wikidata.org/entity/Q42166689

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2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

@en

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

@nl

type

Item

label

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

@en

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

@nl

prefLabel

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

@en

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

@nl

P1476

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme

@en

P2093

Fergal O'Meara

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

John Bradley

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

P2860

PPD v1.0--an integrated, web-accessible database of experimentally determined protein pKa values

The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase

pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds

A simple physical model for binding energy hot spots in protein-protein complexes

Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations

Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints.

Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.

Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy.

Remeasuring HEWL pK(a) values by NMR spectroscopy: methods, analysis, accuracy, and implications for theoretical pK(a) calculations.

Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures.

P304

1636-1645

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

P31

scholarly article

P356

10.1016/J.BPJ.2012.02.048

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P407

English

P433

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

P478

102

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P50

Damien Farrell

J E Nielsen

P577

2012-04-03T00:00:00Z

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

P5875

224034595

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

P698

22500764

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

P932

3318136

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

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

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P2860

P2860

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.

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