Models of S/pi interactions in protein structures: comparison of the H2S benzene complex with PDB data. Export

@article{citeulike:5735991, abstract = {S/pi interactions are prevalent in biochemistry and play an important role in protein folding and stabilization. Geometries of cysteine/aromatic interactions found in crystal structures from the Brookhaven Protein Data Bank (PDB) are analyzed and compared with the equilibrium configurations predicted by high-level quantum mechanical results for the H(2)S-benzene complex. A correlation is observed between the energetically favorable configurations on the quantum mechanical potential energy surface of the H(2)S-benzene model and the cysteine/aromatic configurations most frequently found in crystal structures of the PDB. In contrast to some previous PDB analyses, configurations with the sulfur over the aromatic ring are found to be the most important. Our results suggest that accurate quantum computations on models of noncovalent interactions may be helpful in understanding the structures of proteins and other complex systems.}, author = {Ringer, Ashley L. and Senenko, Anastasia and Sherrill, C. David}, citeulike-article-id = {5735991}, citeulike-linkout-0 = {http://dx.doi.org/10.1110/ps.073002307}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17766371}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17766371}, doi = {10.1110/ps.073002307}, issn = {0961-8368}, journal = {Protein science : a publication of the Protein Society}, keywords = {interface-properties}, month = {October}, number = {10}, pages = {2216--2223}, posted-at = {2009-09-07 18:16:48}, priority = {2}, title = {Models of S/pi interactions in protein structures: comparison of the H2S benzene complex with PDB data.}, url = {http://dx.doi.org/10.1110/ps.073002307}, volume = {16}, year = {2007} }

TY - JOUR ID - citeulike:5735991 L3 - citeulike-article-id:5735991 N2 - S/pi interactions are prevalent in biochemistry and play an important role in protein folding and stabilization. Geometries of cysteine/aromatic interactions found in crystal structures from the Brookhaven Protein Data Bank (PDB) are analyzed and compared with the equilibrium configurations predicted by high-level quantum mechanical results for the H(2)S-benzene complex. A correlation is observed between the energetically favorable configurations on the quantum mechanical potential energy surface of the H(2)S-benzene model and the cysteine/aromatic configurations most frequently found in crystal structures of the PDB. In contrast to some previous PDB analyses, configurations with the sulfur over the aromatic ring are found to be the most important. Our results suggest that accurate quantum computations on models of noncovalent interactions may be helpful in understanding the structures of proteins and other complex systems. IS - 10 JF - Protein science : a publication of the Protein Society SN - 0961-8368 EP - 2223 TI - Models of S/pi interactions in protein structures: comparison of the H2S benzene complex with PDB data. VL - 16 SP - 2216 KW - interface-properties AU - Ringer, Ashley AU - Senenko, Anastasia AU - Sherrill, David PY - 2007/10// UR - http://dx.doi.org/10.1110/ps.073002307 ER -