Literature DB >> 15808225

Elucidation of the protein folding landscape by NMR.

H Jane Dyson1, Peter E Wright.   

Abstract

NMR is one of the few experimental methods that can provide detailed insights into the structure and dynamics of unfolded and partly folded states of proteins. Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding. In addition, it is now recognized that many proteins are intrinsically unstructured in their functional states, while partly folded states of several cellular proteins have been implicated in amyloid disease. NMR is uniquely suited to characterize the structures present in the conformational ensemble and probe the dynamics of the polypeptide chain in unfolded and partially folded protein states.

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Year:  2005        PMID: 15808225     DOI: 10.1016/S0076-6879(05)94011-1

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  29 in total

1.  Folding of the protein domain hbSBD.

Authors:  Maksim Kouza; Chi-Fon Chang; Shura Hayryan; Tsan-hung Yu; Mai Suan Li; Tai-huang Huang; Chin-Kun Hu
Journal:  Biophys J       Date:  2005-08-26       Impact factor: 4.033

2.  Predicting 13Calpha chemical shifts for validation of protein structures.

Authors:  Jorge A Vila; Myriam E Villegas; Hector A Baldoni; Harold A Scheraga
Journal:  J Biomol NMR       Date:  2007-06-09       Impact factor: 2.835

3.  Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics.

Authors:  David B Kony; Philippe H Hünenberger; Wilfred F van Gunsteren
Journal:  Protein Sci       Date:  2007-06       Impact factor: 6.725

Review 4.  An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms.

Authors:  Alice I Bartlett; Sheena E Radford
Journal:  Nat Struct Mol Biol       Date:  2009-06       Impact factor: 15.369

Review 5.  Structural determinants of protein folding.

Authors:  Tse Siang Kang; R Manjunatha Kini
Journal:  Cell Mol Life Sci       Date:  2009-04-15       Impact factor: 9.261

6.  Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.

Authors:  Nils-Alexander Lakomek; Korvin F A Walter; Christophe Farès; Oliver F Lange; Bert L de Groot; Helmut Grubmüller; Rafael Brüschweiler; Axel Munk; Stefan Becker; Jens Meiler; Christian Griesinger
Journal:  J Biomol NMR       Date:  2008-06-04       Impact factor: 2.835

7.  Reduced dimensionality (4,3)D-hnCOCANH experiment: an efficient backbone assignment tool for NMR studies of proteins.

Authors:  Dinesh Kumar
Journal:  J Struct Funct Genomics       Date:  2013-08-27

8.  Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2.

Authors:  Xuecheng Zhang; Matthew A Perugini; Shenggen Yao; Christopher G Adda; Vincent J Murphy; Andrew Low; Robin F Anders; Raymond S Norton
Journal:  J Mol Biol       Date:  2008-03-28       Impact factor: 5.469

Review 9.  Structure-function-folding relationships and native energy landscape of dynein light chain protein: nuclear magnetic resonance insights.

Authors:  P M Krishna Mohan; Ramakrishna V Hosur
Journal:  J Biosci       Date:  2009-09       Impact factor: 1.826

10.  Structural basis for protein antiaggregation activity of the trigger factor chaperone.

Authors:  Tomohide Saio; Xiao Guan; Paolo Rossi; Anastassios Economou; Charalampos G Kalodimos
Journal:  Science       Date:  2014-05-09       Impact factor: 47.728

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