Literature DB >> 9665182

New techniques in structural NMR--anisotropic interactions.

J H Prestegard1.   

Abstract

Structure determination of biomolecules by NMR has traditionally been based on nuclear Overhauser effects (NOEs). Now there are additional sources of information that can complement NOEs in cases where positioning of remote parts of molecules is important, and where extension to larger and more complex systems is desired.

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Year:  1998        PMID: 9665182     DOI: 10.1038/756

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN: 1072-8368


  45 in total

1.  Calculations of NMR dipolar coupling strengths in model peptides.

Authors:  D A Case
Journal:  J Biomol NMR       Date:  1999-10       Impact factor: 2.835

2.  Sign determination of dipolar couplings in field-oriented bicelles by variable angle sample spinning (VASS).

Authors:  F Tian; J A Losonczi; M W Fischer; J H Prestegard
Journal:  J Biomol NMR       Date:  1999-10       Impact factor: 2.835

3.  Assessment of zinc finger orientations by residual dipolar coupling constants.

Authors:  V Tsui; L Zhu; T H Huang; P E Wright; D A Case
Journal:  J Biomol NMR       Date:  2000-01       Impact factor: 2.835

4.  Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings.

Authors:  L G Barrientos; C Dolan; A M Gronenborn
Journal:  J Biomol NMR       Date:  2000-04       Impact factor: 2.835

5.  Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization.

Authors:  G M Clore
Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-01       Impact factor: 11.205

6.  Exact solutions for chemical bond orientations from residual dipolar couplings.

Authors:  William J Wedemeyer; Carol A Rohl; Harold A Scherag
Journal:  J Biomol NMR       Date:  2002-02       Impact factor: 2.835

7.  Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein.

Authors:  W Y Choy; M Tollinger; G A Mueller; L E Kay
Journal:  J Biomol NMR       Date:  2001-09       Impact factor: 2.835

8.  A refined solution structure of hen lysozyme determined using residual dipolar coupling data.

Authors:  H Schwalbe; S B Grimshaw; A Spencer; M Buck; J Boyd; C M Dobson; C Redfield; L J Smith
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

9.  Automated protein fold determination using a minimal NMR constraint strategy.

Authors:  Deyou Zheng; Yuanpeng J Huang; Hunter N B Moseley; Rong Xiao; James Aramini; G V T Swapna; Gaetano T Montelione
Journal:  Protein Sci       Date:  2003-06       Impact factor: 6.725

Review 10.  Utilizing NMR to study the structure of growth-inhibitory proteins.

Authors:  Francesca Marassi
Journal:  Methods Mol Biol       Date:  2003
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