Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding (Q46430110)

22 December 2017

title

Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding (English)

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22 December 2017

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David Wildes

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22 December 2017

Susan Marqusee

series ordinal

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22 December 2017

language of work or name

English

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publication date

1 January 2004

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22 December 2017

published in

Methods in Enzymology

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22 December 2017

volume

380

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22 December 2017

page(s)

328-349

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22 December 2017

Hydrogen exchange and structural dynamics of proteins and nucleic acids

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Kinetics and thermodynamics of conformational equilibria in native proteins by hydrogen exchange

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Primary structure effects on peptide group hydrogen exchange

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Rate and equilibrium constants for protein unfolding and refolding determined by hydrogen exchange-mass spectrometry

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Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry

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Hydrogen exchange and protein folding.

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Protein folding intermediates and pathways studied by hydrogen exchange

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Hydrogen exchange studies of protein structure

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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7 January 2021

Protein conformational stabilities can be determined from hydrogen exchange rates

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A.

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Protein folding intermediates: native-state hydrogen exchange

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Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH.

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Protein hydrogen exchange mechanism: local fluctuations

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Ensemble modulation as an origin of denaturant-independent hydrogen exchange in proteins

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Solvent isotope effect and protein stability

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Folding Dynamics of the src SH3 Domain

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Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation

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7 January 2021

Evolutionarily conserved pathways of energetic connectivity in protein families

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The linkage between protein folding and functional cooperativity: two sides of the same coin?

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Structure and energy change in hemoglobin by hydrogen exchange labeling

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Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR

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An Antibody Binding Site on Cytochrome C Defined by Hydrogen Exchange and Two-Dimensional NMR

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The role of backbone motions in ligand binding to the c-Src SH3 domain

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Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

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7 January 2021

Natively unfolded proteins: a point where biology waits for physics

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7 January 2021

A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution.

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7 January 2021

Hydrogen Exchange in Proteins

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7 January 2021

10.1016/S0076-6879(04)80015-6

Identifiers

DOI

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22 December 2017

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22 December 2017