Cis-trans isomerizations of proline residues are key to bradykinin conformations.
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ABSTRACT:
SUBMITTER: Pierson NA
PROVIDER: S-EPMC3624761 | biostudies-literature | 2013 Feb
REPOSITORIES: biostudies-literature
Publications
Cis-trans isomerizations of proline residues are key to bradykinin conformations.
Pierson Nicholas A NA Chen Liuxi L Russell David H DH Clemmer David E DE
Journal of the American Chemical Society 20130213 8
A recent ion mobility-mass spectrometry (IM-MS) study of the nonapeptide bradykinin (BK, amino acid sequence Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)) found evidence for 10 populations of conformations that depend upon the solution composition [J. Am. Chem. Soc. 2011, 133, 13810]. Here, the role of the three proline residues (Pro(2), Pro(3), and Pro(7)) in establishing these conformations is investigated using a series of seven analogue peptides in which combinations of ala ...[more]
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