Quantifying amino acid conformational preferences and side-chain–side-chain interactions in β-hairpins Export

@article{citeulike:621357, abstract = {10.1073/pnas.0506646102 The intrinsic conformational biases of individual amino acids and their interstrand side-chain–side-chain (SC–SC) interactions both contribute to the stability of β-sheets. The relative magnitudes of these effects have been difficult to assess in the context of folded proteins, where tertiary contacts complicate the quantitative analysis of local effects. We now report the results of such an analysis in a much simpler system, a short, stabilized β-hairpin structure where intrastrand (conformational) and interstrand (SC–SC) influences can be distinguished in the absence of competing protein tertiary interactions. A comprehensive comparison of all pairwise combinations of 11 N-terminal and 7 C-terminal amino acids within an 8-residue, @-tide-stabilized [in which @ denotes the 1,2-dihydro-3(6)-pyridinyl unit] β-hairpin reveals distinct differences between the various pairings and shows that the intrastrand and interstrand effects are of comparable magnitude in contributing to the stability of the folded forms over the unfolded forms.}, address = {Center for New Directions in Organic Synthesis, Department of Chemistry, University of California, Berkeley, CA 94720-1460, USA.}, author = {Phillips, Scott T. and Piersanti, Giovanni and Bartlett, Paul A.}, citeulike-article-id = {621357}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0506646102}, citeulike-linkout-1 = {http://www.pnas.org/content/102/39/13737.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/102/39/13737.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/16162669}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=16162669}, day = {27}, doi = {10.1073/pnas.0506646102}, issn = {0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {beta-hairpin, beta-strand, conformation, sequence-structure}, month = {September}, number = {39}, pages = {13737--13742}, posted-at = {2006-05-10 14:28:07}, priority = {2}, title = {Quantifying amino acid conformational preferences and side-chain–side-chain interactions in β-hairpins}, url = {http://dx.doi.org/10.1073/pnas.0506646102}, volume = {102}, year = {2005} }

TY - JOUR ID - citeulike:621357 L3 - citeulike-article-id:621357 N2 - 10.1073/pnas.0506646102 The intrinsic conformational biases of individual amino acids and their interstrand side-chain–side-chain (SC–SC) interactions both contribute to the stability of β-sheets. The relative magnitudes of these effects have been difficult to assess in the context of folded proteins, where tertiary contacts complicate the quantitative analysis of local effects. We now report the results of such an analysis in a much simpler system, a short, stabilized β-hairpin structure where intrastrand (conformational) and interstrand (SC–SC) influences can be distinguished in the absence of competing protein tertiary interactions. A comprehensive comparison of all pairwise combinations of 11 N-terminal and 7 C-terminal amino acids within an 8-residue, @-tide-stabilized [in which @ denotes the 1,2-dihydro-3(6)-pyridinyl unit] β-hairpin reveals distinct differences between the various pairings and shows that the intrastrand and interstrand effects are of comparable magnitude in contributing to the stability of the folded forms over the unfolded forms. IS - 39 JF - Proceedings of the National Academy of Sciences of the United States of America SN - 0027-8424 AD - Center for New Directions in Organic Synthesis, Department of Chemistry, University of California, Berkeley, CA 94720-1460, USA. EP - 13742 TI - Quantifying amino acid conformational preferences and side-chain–side-chain interactions in β-hairpins VL - 102 SP - 13737 KW - beta-hairpin KW - beta-strand KW - conformation KW - sequence-structure AU - Phillips, Scott AU - Piersanti, Giovanni AU - Bartlett, Paul PY - 2005/09/27/ UR - http://dx.doi.org/10.1073/pnas.0506646102 ER -