(Q30426755)

21 June 2017

title

An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway (English)

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21 June 2017

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2

Fersht AR

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21 June 2017

Clarke J

1

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21 June 2017

publication date

1 January 1996

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21 June 2017

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21 June 2017

volume

1

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21 June 2017

issue

4

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21 June 2017

page(s)

243-254

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Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance

21 June 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2896%2900038-7

7 January 2021

Hydrogen exchange and structural dynamics of proteins and nucleic acids

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7 January 2021

A nuclear magnetic resonance study of the hydrogen-exchange behaviour of lysozyme in crystals and solution

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7 January 2021

Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution

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7 January 2021

Hydrogen exchange in native and denatured states of hen egg-white lysozyme

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Hydrogen exchange identifies native-state motional domains important in protein folding

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7 January 2021

Hydrogen Exchange in Proteins

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Hydrogen Exchange Kinetics and Internal Motions in Proteins and Nucleic Acids

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7 January 2021

Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.

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7 January 2021

Stable submolecular folding units in a non-compact form of cytochrome c

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7 January 2021

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

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7 January 2021

Protein folding intermediates: native-state hydrogen exchange

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7 January 2021

Protein stability parameters measured by hydrogen exchange

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7 January 2021

Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways

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7 January 2021

Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.

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The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure

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7 January 2021

Protein hydrogen exchange in denaturant: quantitative analysis by a two-process model

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7 January 2021

Correlation of hydrogen exchange behaviour and thermal stability of lysozyme

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7 January 2021

Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor

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7 January 2021

Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor

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7 January 2021

A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions

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7 January 2021

Primary structure effects on peptide group hydrogen exchange

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7 January 2021

Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation

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7 January 2021

Primary structure effects on peptide group hydrogen exchange.

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7 January 2021

Detection of transient protein folding populations by mass spectrometry

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7 January 2021

Nuclear magnetic resonance studies of the internal dynamics in Apo, (Cd2+)1 and (Ca2+)2 calbindin D9k. The rates of amide proton exchange with solvent

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7 January 2021

Isotope effects in peptide group hydrogen exchange

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7 January 2021

Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state

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7 January 2021

A statistical mechanical model for hydrogen exchange in globular proteins

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7 January 2021

Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR.

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7 January 2021

Is the slow exchange core the protein folding core?

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7 January 2021

Molecular structure of a new family of ribonucleases

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7 January 2021

10.1016/S1359-0278(96)00038-7

Identifiers

DOI

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21 June 2017

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