These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Addition of side chains to a known backbone with defined side-chain centroids.
    Author: Kaźmierkiewicz R, Liwo A, Scheraga HA.
    Journal: Biophys Chem; 2003; 100(1-3):261-80. PubMed ID: 12646370.
    Abstract:
    An automatic procedure is proposed for adding side chains to a protein backbone; it is based on optimization of a simplified energy function for peptide side chains, given its backbone and positions of side-chain centroids. The energy is expressed as a sum of the energies of interaction between side chains, and a harmonic penalty function accounting for the preservation of the positions of the C(alpha) atoms and the side-chain centroids. The energy of side-chain interactions is calculated with the soft-sphere ECEPP/3 potential. A Monte Carlo search is carried out to explore all possible side-chain orientations within a fixed backbone and side-chain centroid positions. The initial, usually extended, side-chain conformations are taken directly from the ECEPP/3 database. The procedure was tested on six experimental (X-ray or NMR) structures: immunoglobulin binding protein (PDB code 1IGD, an alpha+beta-protein); transcription factor PML (PDB code 1BOR, a 49-104 fragment of the ring finger domain, predominantly beta-protein); bovine pancreatic trypsin inhibitor (crystal form II) (PDB code 1BPI, an alpha+beta-protein); the monomer of human deoxyhemoglobin (PDB code 1BZ0, an alpha-helical structure); chain A of alcohol dehydrogenase from Drosophila lebanonensis (PDB code 1A4U); as well as on the 10-55 portion of the B domain of staphylococcal protein A (PDB code 1BDD). In all cases except 1BPI, the data for the algorithm (i.e. the backbone or C(alpha) coordinates and the positions of side-chain centroids) were taken from the experimental structures. For protein A, the C(alpha) coordinates and positions of side-chain centroids were also taken from the 1.9-A-resolution model predicted by the UNRES force field. In all comparisons with experimental structures, complete side-chain geometry was reconstructed with a root-mean-square (RMS) deviation of approximately 0.6-0.9 A from the heavy atoms when complete backbone and side-chain-centroid coordinates were used in reconstruction, or approximately 1.0 A when the C(alpha) and centroid coordinates were used.
    [Abstract] [Full Text] [Related] [New Search]