Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling (Q73175489)

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1 November 2019

title

Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling (English)

1 reference

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1 November 2019

author name string

Gladwin ST

series ordinal

1

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1 November 2019

Evans PA

series ordinal

2

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1 November 2019

publication date

1 January 1996

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1 November 2019

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1 November 2019

volume

1

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1 November 2019

issue

6

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1 November 2019

page(s)

407-417

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Experimental investigation of sidechain interactions in early folding intermediates

1 November 2019

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Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR

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The folding of hen lysozyme involves partially structured intermediates and multiple pathways

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Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme

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Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism

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Early hydrogen-bonding events in the folding reaction of ubiquitin

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Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues

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Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin

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Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin

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Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange

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Effects of denaturants on amide proton exchange rates: a test for structure in protein fragments and folding intermediates

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Primary structure effects on peptide group hydrogen exchange

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

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Amide hydrogen exchange in a highly denatured state. Hen egg-white lysozyme in urea

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Conformational Properties of Four Peptides Spanning the Sequence of Hen Lysozyme

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Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study

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Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates

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Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotometry

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7 January 2021

On the Conformation of the Hen Egg-White Lysozyme Molecule

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Identifiers

DOI

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1 November 2019

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