Progress in structure prediction of α-helical membrane proteins Export

@article{citeulike:771145, abstract = {Transmembrane (TM) proteins comprise 20-30\% of the genome but, because of experimental difficulties, they represent less than 1\% of the Protein Data Bank. The dearth of membrane protein structures makes computational prediction a potentially important means of obtaining novel structures. Recent advances in computational methods have been combined with experimental data to constrain the modeling of three-dimensional structures. Furthermore, threading and ab initio modeling approaches that were effective for soluble proteins have been applied to TM domains. Surprisingly, experimental structures, proteomic analyses and bioinformatics have revealed unexpected architectures that counter long-held views on TM protein structure and stability. Future computational and experimental studies aimed at understanding the thermodynamic and evolutionary bases of these architectural details will greatly enhance predictive capabilities.}, address = {Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University Ramat Aviv 69978, Israel.}, author = {Fleishman, S. and Bental, N.}, citeulike-article-id = {771145}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.sbi.2006.06.003}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0959440X06001072}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/16822664}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=16822664}, day = {3}, doi = {10.1016/j.sbi.2006.06.003}, issn = {0959440X}, journal = {Current Opinion in Structural Biology}, keywords = {alpha-helices, membrane\_protein, structure\_prediction}, month = {August}, number = {4}, pages = {496--504}, posted-at = {2009-11-11 16:20:15}, priority = {2}, title = {Progress in structure prediction of α-helical membrane proteins}, url = {http://dx.doi.org/10.1016/j.sbi.2006.06.003}, volume = {16}, year = {2006} }

TY - JOUR ID - citeulike:771145 L3 - citeulike-article-id:771145 N2 - Transmembrane (TM) proteins comprise 20-30% of the genome but, because of experimental difficulties, they represent less than 1% of the Protein Data Bank. The dearth of membrane protein structures makes computational prediction a potentially important means of obtaining novel structures. Recent advances in computational methods have been combined with experimental data to constrain the modeling of three-dimensional structures. Furthermore, threading and ab initio modeling approaches that were effective for soluble proteins have been applied to TM domains. Surprisingly, experimental structures, proteomic analyses and bioinformatics have revealed unexpected architectures that counter long-held views on TM protein structure and stability. Future computational and experimental studies aimed at understanding the thermodynamic and evolutionary bases of these architectural details will greatly enhance predictive capabilities. IS - 4 JF - Current Opinion in Structural Biology SN - 0959440X AD - Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University Ramat Aviv 69978, Israel. EP - 504 TI - Progress in structure prediction of α-helical membrane proteins VL - 16 SP - 496 KW - alpha-helices KW - membrane_protein KW - structure_prediction AU - Fleishman, S AU - Bental, N PY - 2006/08/03/ UR - http://dx.doi.org/10.1016/j.sbi.2006.06.003 ER -