The use of 1JC?H? coupling constants as a probe for protein backbone conformation

1993 ◽  
Vol 3 (1) ◽  
Author(s):  
GeertenW. Vuister ◽  
Frank Delaglio ◽  
Ad Bax
Keyword(s):  
Coupling Constants ◽  
Protein Backbone ◽  
Backbone Conformation ◽  
Protein Backbone Conformation

scholarly journals Knowledge-based prediction of protein backbone conformation using a structural alphabet

PLoS ONE ◽  
2017 ◽  
Vol 12 (11) ◽  
pp. e0186215 ◽  
Author(s):  
Iyanar Vetrivel ◽  
Swapnil Mahajan ◽  
Manoj Tyagi ◽  
Lionel Hoffmann ◽  
Yves-Henri Sanejouand ◽  
...  
Keyword(s):  
Protein Backbone ◽  
Structural Alphabet ◽  
Knowledge Based ◽  
Backbone Conformation ◽  
Protein Backbone Conformation

Prediction of protein backbone conformation based on seven structure assignments

1991 ◽  
Vol 221 (3) ◽  
pp. 961-979 ◽  
Author(s):  
Marianne J. Rooman ◽  
Jean-Pierre A. Kocher ◽  
Shoshana J. Wodak
Keyword(s):  
Protein Backbone ◽  
Backbone Conformation ◽  
Protein Backbone Conformation

scholarly journals Investigation of the impact of PTMs on the protein backbone conformation

Amino Acids ◽  
2019 ◽  
Vol 51 (7) ◽  
pp. 1065-1079 ◽  
Author(s):  
Pierrick Craveur ◽  
Tarun J. Narwani ◽  
Joseph Rebehmed ◽  
Alexandre G. de Brevern
Keyword(s):  
Protein Backbone ◽  
Backbone Conformation ◽  
The Impact ◽  
Protein Backbone Conformation

scholarly journals A new default restraint library for the protein backbone inPhenix: a conformation-dependent geometry goes mainstream

2016 ◽  
Vol 72 (1) ◽  
pp. 176-179 ◽  
Author(s):  
Nigel W. Moriarty ◽  
Dale E. Tronrud ◽  
Paul D. Adams ◽  
P. Andrew Karplus
Keyword(s):  
Protein Structure ◽  
Protein Data Bank ◽  
Transition Period ◽  
Structure Refinement ◽  
Data Bank ◽  
Protein Backbone ◽  
Protein Structure Refinement ◽  
Fundamental Part ◽  
Backbone Conformation ◽  
Protein Backbone Conformation

Chemical restraints are a fundamental part of crystallographic protein structure refinement. In response to mounting evidence that conventional restraints have shortcomings, it has previously been documented that using backbone restraints that depend on the protein backbone conformation helps to address these shortcomings and improves the performance of refinements [Moriartyet al.(2014),FEBS J.281, 4061–4071]. It is important that these improvements be made available to all in the protein crystallography community. Toward this end, a change in the default geometry library used byPhenixis described here. Tests are presented showing that this change will not generate increased numbers of outliers during validation, or deposition in the Protein Data Bank, during the transition period in which some validation tools still use the conventional restraint libraries.

Pulse Sequences for Measurement of One-Bond 15N–1H Coupling Constants in the Protein Backbone

1999 ◽  
Vol 140 (1) ◽  
pp. 259-263 ◽  
Author(s):  
Mathilde H. Lerche ◽  
Axel Meissner ◽  
Flemming M. Poulsen ◽  
Ole Winneche Sørensen
Keyword(s):  
Pulse Sequences ◽  
Coupling Constants ◽  
Protein Backbone
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