Helix capping propensities in peptides parallel those in proteins.

@article{chakrabartty1993, abstract = {Helix content of peptides with various uncharged nonaromatic amino acids at either the N-terminal or C-terminal position has been determined. The choice of N-terminal amino acid has a major effect on helix stability: asparagine is the best, glycine is very good, and glutamine is the worst helix-stabilizing amino acid at this position. The rank order of helix stabilization parallels the frequencies of these amino acids at the N-terminal boundary (N-cap) position of helices in proteins found by Richardson and Richardson [Richardson, J. S. \& Richardson, D. C. (1988) Science 240, 1648-1652], and the N-terminal amino acid in a peptide composed of helix-forming amino acids may be considered as the N-cap residue. The choice of C-terminal amino acid has only a minor effect on helix stability. N-capping interactions may be responsible for the asymmetric distribution of helix content within a given peptide found by various workers. An acetyl group on the N-terminal alpha-amino function cancels the N-cap effect and the acetyl group is equivalent to N-terminal asparagine in an unacetylated peptide. Our results demonstrate a close relationship between the mechanisms of alpha-helix formation in peptides and in proteins.}, address = {Department of Biochemistry, Beckman Center, Stanford University Medical School, CA 94305-5307.}, author = {Chakrabartty, A. and Doig, A. J. and Baldwin, R. L. }, citeulike-article-id = {326813}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {chakrabartty1993}, month = {December}, number = {23}, pages = {11332--11336}, posted-at = {2008-04-07 10:30:37}, priority = {2}, title = {Helix capping propensities in peptides parallel those in proteins.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8248248}, volume = {90}, year = {1993} }

TY - JOUR ID - chakrabartty1993 L3 - citeulike-article-id:326813 TI - Helix capping propensities in peptides parallel those in proteins. JF - Proc Natl Acad Sci U S A VL - 90 IS - 23 SP - 11332 EP - 11336 AD - Department of Biochemistry, Beckman Center, Stanford University Medical School, CA 94305-5307. SN - 0027-8424 N2 - Helix content of peptides with various uncharged nonaromatic amino acids at either the N-terminal or C-terminal position has been determined. The choice of N-terminal amino acid has a major effect on helix stability: asparagine is the best, glycine is very good, and glutamine is the worst helix-stabilizing amino acid at this position. The rank order of helix stabilization parallels the frequencies of these amino acids at the N-terminal boundary (N-cap) position of helices in proteins found by Richardson and Richardson [Richardson, J. S. & Richardson, D. C. (1988) Science 240, 1648-1652], and the N-terminal amino acid in a peptide composed of helix-forming amino acids may be considered as the N-cap residue. The choice of C-terminal amino acid has only a minor effect on helix stability. N-capping interactions may be responsible for the asymmetric distribution of helix content within a given peptide found by various workers. An acetyl group on the N-terminal alpha-amino function cancels the N-cap effect and the acetyl group is equivalent to N-terminal asparagine in an unacetylated peptide. Our results demonstrate a close relationship between the mechanisms of alpha-helix formation in peptides and in proteins. KW - chakrabartty1993 AU - Chakrabartty, A AU - Doig, AJ AU - Baldwin, RL PY - 1993/12/01/ UR - http://view.ncbi.nlm.nih.gov/pubmed/8248248 ER -