Analysis of side-chain rotamers in transmembrane proteins. Export

@article{citeulike:2801264, abstract = {We measured the frequency of side-chain rotamers in 14 alpha-helical and 16 beta-barrel membrane protein structures and found that the membrane environment considerably perturbs the rotamer frequencies compared to soluble proteins. Although there are limited experimental data, we found statistically significant changes in rotamer preferences depending on the residue environment. Rotamer distributions were influenced by whether the residues were lipid or protein facing, and whether the residues were found near the N- or C-terminus. Hydrogen-bonding interactions with the helical backbone perturbs the rotamer populations of Ser and His. Trp and Tyr favor side-chain conformations that allow their side chains to extend their polar atoms out of the membrane core, thereby aligning the side-chain polarity gradient with the polarity gradient of the membrane. Our results demonstrate how the membrane environment influences protein structures, providing information that will be useful in the structure prediction and design of transmembrane proteins.}, address = {Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, California 90095-1570, USA.}, author = {Chamberlain, A. K. and Bowie, J. U.}, citeulike-article-id = {2801264}, citeulike-linkout-0 = {http://dx.doi.org/10.1529/biophysj.104.044024}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15339811}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15339811}, doi = {10.1529/biophysj.104.044024}, issn = {0006-3495}, journal = {Biophysical journal}, keywords = {flexibility, hbond, helix, membrane\_proteins, ser, structure, thr, transmembrane}, month = {November}, number = {5}, pages = {3460--3469}, posted-at = {2008-05-15 11:35:47}, priority = {2}, title = {Analysis of side-chain rotamers in transmembrane proteins.}, url = {http://dx.doi.org/10.1529/biophysj.104.044024}, volume = {87}, year = {2004} }

TY - JOUR ID - citeulike:2801264 L3 - citeulike-article-id:2801264 N2 - We measured the frequency of side-chain rotamers in 14 alpha-helical and 16 beta-barrel membrane protein structures and found that the membrane environment considerably perturbs the rotamer frequencies compared to soluble proteins. Although there are limited experimental data, we found statistically significant changes in rotamer preferences depending on the residue environment. Rotamer distributions were influenced by whether the residues were lipid or protein facing, and whether the residues were found near the N- or C-terminus. Hydrogen-bonding interactions with the helical backbone perturbs the rotamer populations of Ser and His. Trp and Tyr favor side-chain conformations that allow their side chains to extend their polar atoms out of the membrane core, thereby aligning the side-chain polarity gradient with the polarity gradient of the membrane. Our results demonstrate how the membrane environment influences protein structures, providing information that will be useful in the structure prediction and design of transmembrane proteins. IS - 5 JF - Biophysical journal SN - 0006-3495 AD - Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, California 90095-1570, USA. EP - 3469 TI - Analysis of side-chain rotamers in transmembrane proteins. VL - 87 SP - 3460 KW - flexibility KW - hbond KW - helix KW - membrane_proteins KW - ser KW - structure KW - thr KW - transmembrane AU - Chamberlain, AK AU - Bowie, JU PY - 2004/11// UR - http://dx.doi.org/10.1529/biophysj.104.044024 ER -