Defining an essence of structure determining residue contacts in proteins.

ABSTRACT: The network of native non-covalent residue contacts determines the three-dimensional structure of a protein. However, not all contacts are of equal structural significance, and little knowledge exists about a minimal, yet sufficient, subset required to define the global features of a protein. Characterisation of this "structural essence" has remained elusive so far: no algorithmic strategy has been devised to-date that could outperform a random selection in terms of 3D reconstruction accuracy (measured as the Ca RMSD). It is not only of theoretical interest (i.e., for design of advanced statistical potentials) to identify the number and nature of essential native contacts-such a subset of spatial constraints is very useful in a number of novel experimental methods (like EPR) which rely hea

SUBMITTER: Sathyapriya R 

PROVIDER: S-EPMC2778133 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature