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Solution structure of αtα, a helical hairpin peptide of de novo design
Author(s) -
Fezoui Youcef,
Connolly Peter J.,
Osterhout John J.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060907
Subject(s) - dihedral angle , peptide , crystallography , protein structure , chemistry , residue (chemistry) , physics , nuclear magnetic resonance , molecule , biochemistry , hydrogen bond , organic chemistry
αtα is a 38‐residue peptide designed to adopt a helical hairpin conformation in solution (Fezoui Y, Weaver DL, Osterhout JJ, 1995, Protein Sci 4286‐295). A previous study of the carboxylate form of αtα by CD and two‐dimensional NMR indicated that the peptide was highly helical and that the helices associated in approximately the intended orientation (Fezoui Y, Weaver DL, Osterhout JJ, 1994, Proc Natl Acad Sci USA 91:3675‐3679). Here, the solution structure of αtα as determined by two‐dimensional NMR is reported. A total of 266 experimentally derived distance restraints and 20 dihedral angle restraints derived from J‐couplings were used. One‐hundred initial structures were generated by distance geometry and refined by dynamical simulated annealing. Twenty‐three of the lowest‐energy structures consistent with the experimental restraints were analyzed. The results presented here show that αtα is comprised of two associating helices connected by a turn region.