The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding. Export

@article{citeulike:802650, abstract = {Using an all-atom representation, we exhaustively enumerate all sterically allowed conformations for short polyalanyl chains. Only intrachain interactions are considered, including one adjustable parameter, a favorable backbone energy (e.g., a peptide hydrogen bond). The counting is used to reevaluate Flory's isolated-pair hypothesis, the simplifying assumption that each phi,psi pair is sterically independent. This hypothesis is a conceptual linchpin in helix-coil theories and protein folding. Contrary to the hypothesis, we find that systematic local steric effects can extend beyond nearest-chain neighbors and can restrict the size of accessible conformational space significantly. As a result, the entropy price that must be paid to adopt any specific conformation is far less than previously thought.}, address = {Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.}, author = {Pappu, R. V. and Srinivasan, R. and Rose, G. D.}, citeulike-article-id = {802650}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.97.23.12565}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11070081}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11070081}, day = {7}, doi = {10.1073/pnas.97.23.12565}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {d4, dihedrals, flory, folding}, month = {November}, number = {23}, pages = {12565--12570}, posted-at = {2006-12-20 12:15:59}, priority = {2}, title = {The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding.}, url = {http://dx.doi.org/10.1073/pnas.97.23.12565}, volume = {97}, year = {2000} }

TY - JOUR ID - citeulike:802650 L3 - citeulike-article-id:802650 N2 - Using an all-atom representation, we exhaustively enumerate all sterically allowed conformations for short polyalanyl chains. Only intrachain interactions are considered, including one adjustable parameter, a favorable backbone energy (e.g., a peptide hydrogen bond). The counting is used to reevaluate Flory's isolated-pair hypothesis, the simplifying assumption that each phi,psi pair is sterically independent. This hypothesis is a conceptual linchpin in helix-coil theories and protein folding. Contrary to the hypothesis, we find that systematic local steric effects can extend beyond nearest-chain neighbors and can restrict the size of accessible conformational space significantly. As a result, the entropy price that must be paid to adopt any specific conformation is far less than previously thought. IS - 23 JF - Proc Natl Acad Sci U S A SN - 0027-8424 AD - Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA. EP - 12570 TI - The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding. VL - 97 SP - 12565 KW - d4 KW - dihedrals KW - flory KW - folding AU - Pappu, RV AU - Srinivasan, R AU - Rose, GD PY - 2000/11/07/ UR - http://dx.doi.org/10.1073/pnas.97.23.12565 ER -