Equilibrium NMR studies of unfolded and partially folded proteins (Q46162800)

20 December 2017

review article

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title

Equilibrium NMR studies of unfolded and partially folded proteins (English)

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20 December 2017

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1

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20 December 2017

Peter Wright

series ordinal

2

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20 December 2017

publication date

1 July 1998

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20 December 2017

Nature structural biology

published in

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20 December 2017

volume

5 Suppl

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20 December 2017

page(s)

499-503

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20 December 2017

Insights into protein folding from NMR.

cites work

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Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

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Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins

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Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study

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Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding

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Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding

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Chemical shifts as a tool for structure determination

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Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations

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The concept of a random coil. Residual structure in peptides and denatured proteins

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NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions

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Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin

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Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Delta131Delta, using NMR methods with improved resolution.

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

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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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Backbone dynamics and structural characterization of the partially folded A state of ubiquitin by 1H, 13C, and 15N nuclear magnetic resonance spectroscopy

21 January 2018

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Characterization of the backbone dynamics of folded and denatured states of an SH3 domain

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Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.

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Cell biology. The importance of being unfolded.

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Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions

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Folding of peptide fragments comprising the complete sequence of proteins

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Sequence-Corrected 15N "Random Coil" Chemical Shifts

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A residue-specific NMR view of the non-cooperative unfolding of a molten globule

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NMR determination of residual structure in a urea-denatured protein, the 434-repressor

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NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein

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NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A

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Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride

21 January 2018

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7 January 2021

Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin

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7 January 2021

Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor

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7 January 2021

Structural characterization of a partly folded apomyoglobin intermediate

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7 January 2021

Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels

1 reference

7 January 2021

Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures

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7 January 2021

Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease

1 reference

7 January 2021

The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations

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7 January 2021

Identifiers

DOI

10.1038/739

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20 December 2017

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20 December 2017