(Q27664400)

4

object named as

Alan R Fersht

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author name string

Dmitry M Korzhnev

1

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Tomasz L Religa

2

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Wiktor Banachewicz

Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy

3

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language of work or name

English

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publication date

10 September 2010

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published in

Science

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volume

329

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page(s)

1312-6

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issue

5997

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cites work

1 reference

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Consistent blind protein structure generation from NMR chemical shift data

21 April 2017

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CS23D: a web server for rapid protein structure generation using NMR chemical shifts and sequence data

21 April 2017

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The structure of an FF domain from human HYPA/FBP11

21 April 2017

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Mapping the transition state and pathway of protein folding by protein engineering

21 April 2017

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Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

21 April 2017

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TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

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NMR structure determination for larger proteins using backbone-only data

21 April 2017

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The helix turn helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain

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Macromolecular modeling with rosetta

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Intermediates: ubiquitous species on folding energy landscapes?

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The present view of the mechanism of protein folding

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Protein Folding: A Perspective from Theory and Experiment.

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Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.

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Solution structure of a protein denatured state and folding intermediate.

21 January 2018

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Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding

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NMR spectroscopy brings invisible protein states into focus

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Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules

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Measurement of bond vector orientations in invisible excited states of proteins

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Characterization of chemical exchange using residual dipolar coupling

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Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy

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Protein structure determination from NMR chemical shifts

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Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation

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The structure of the major transition state for folding of an FF domain from experiment and simulation

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Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain

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Carbonyl carbon transverse relaxation dispersion measurements and ms-micros timescale motion in a protein hydrogen bond network

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Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy

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Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples

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Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments

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Use of chemical shifts in macromolecular structure determination

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A simple method to predict protein flexibility using secondary chemical shifts

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A protein folding pathway with multiple folding intermediates at atomic resolution

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Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family

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Zebrafish get ordered: new doors open for imaging membrane organization

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Protein folding and misfolding: mechanism and principles.

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Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins

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Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology

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Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients

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Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in proteins

21 January 2018

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An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins

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Probing Chemical Shifts of Invisible States of Proteins with Relaxation Dispersion NMR Spectroscopy: How Well Can We Do?

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21 January 2018

Identifiers

DOI

10.1126/SCIENCE.1191723

1 reference

Consolidated OpenCitations Corpus – April 2017

837806

837806

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference