Modeling of denatured state for calculation of the electrostatic contribution to protein stability.

Modeling of denatured state for calculation of the electrostatic contribution to protein stability.

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http://www.wikidata.org/entity/Q38270088
Site-specific contributions to the pH dependence of protein stabilityPredicting folding free energy changes upon single point mutationsThe N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.Rational modification of protein stability by targeting surface sites leads to complicated resultsElectrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles.Studying the role of cooperative hydration in stabilizing folded protein states.Strategies for a direct characterization of phosphoproteins on hydroxyapatite surfaces.Structure-based pKa calculations using continuum electrostatics methods.Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.
P2860

Modeling of denatured state for calculation of the electrostatic contribution to protein stability.

Item
http://www.wikidata.org/entity/Q38270088
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2002 nî lūn-bûn
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name
Modeling of denatured state fo ...... ribution to protein stability.
@en
type
label
Modeling of denatured state fo ...... ribution to protein stability.
@en
prefLabel
Modeling of denatured state fo ...... ribution to protein stability.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Modeling of denatured state fo ...... ribution to protein stability.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932