Literature DB >> 8581305

Carbonyl-carbon relaxation rates reveal a dynamic heterogeneity of the polypeptide backbone in villin 14T.

K T Dayie1, G Wagner.   

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Year:  1995        PMID： 8581305     DOI： 10.1006/jmrb.1995.1155

Source DB:  PubMed          Journal:  J Magn Reson B        ISSN： 1064-1866


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  4 in total

1.  Correlated motions of successive amide N-H bonds in proteins.

Authors:  Philippe Pelupessy; Sapna Ravindranathan; Geoffrey Bodenhausen
Journal:  J Biomol NMR       Date:  2003-04       Impact factor: 2.835

2.  Refinement of protein structure against non-redundant carbonyl 13C NMR relaxation.

Authors:  Nico Tjandra; Motoshi Suzuki; Shou-Lin Chang
Journal:  J Biomol NMR       Date:  2007-06-07       Impact factor: 2.835

3.  Characterizing semilocal motions in proteins by NMR relaxation studies.

Authors:  M W Fischer; L Zeng; A Majumdar; E R Zuiderweg
Journal:  Proc Natl Acad Sci U S A       Date:  1998-07-07       Impact factor: 11.205

4.  Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1.

Authors:  J Engelke; H Rüterjans
Journal:  J Biomol NMR       Date:  1997-01       Impact factor: 2.835
  4 in total

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