Biomedical Engineering Reference
In-Depth Information
CHAPTER 8
Residual Dipolar Couplings as a
Tool for the Study of Protein
Conformation and
Conformational Flexibility
LO ยจ C SALMON a , PHINEUS MARKWICK b
AND
MARTIN BLACKLEDGE* a
a Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre
Ebel, CEA, CNRS, UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027,
France; b Department of Chemistry and Biochemistry, University of California
San Diego, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA
*E-mail: martin.blackledge@ibs.fr
8.1 Introduction
The determination of the three-dimensional structure of biomolecules has
contributed enormously to our understanding of biology, giving access to
atomic-resolution descriptions of the molecular basis of functionally important
interactions between biochemically active molecules. 1,2 Proteins are however
intrinsically dynamic, exhibiting a flexibility that can be manifest in terms of
large-scale re-organisations or small-scale conformational fluctuations of
backbone and side-chain atoms about their mean conformation, 3,4 and it is
becoming increasingly apparent that a full understanding of biomolecular
function requires a description of the nature and role of the conformational
dynamics of the protein. Despite this realisation, three-dimensional protein
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