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Calcium-binding properties and molecular organization of bradykinin A solution 1H-NMR study.

Gaggelli, E; D'amelio, N; MacCotta, A; Valensin, G; (1999) Calcium-binding properties and molecular organization of bradykinin A solution 1H-NMR study. Eur J Biochem , 262 (2) pp. 268-276.

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Abstract

The NMR features of bradykinin were investigated in dimethylsulfoxide containing 1% water. The temperature dependence of chemical shifts and ROESY maps were monitored for the major species where all X-Pro bonds are trans. The occurrence of a head-to-tail ionic interaction and intramolecular hydrogen bonds stabilizing a pseudo cyclic arrangement was inferred, a beta turn at the C-terminus being the main feature of the secondary structure. Calcium was shown to bind to the peptide with a dissociation constant Kd = 2.8 + 0.2 mm. 2Pro and 3Pro carbonyls, as well as the 9Arg carboxyl, were assigned as the metal-binding sites. A molecular model of the 1 : 1 metal-complex was obtained. In light of conformational changes experienced by the peptide upon interaction with calcium, a role for the metal was hypothesized in the process of conformational selection from the free to the receptor-bound state of bradykinin.

Type: Article
Title: Calcium-binding properties and molecular organization of bradykinin A solution 1H-NMR study.
Location: England
Keywords: Bradykinin, Calcium, Hydrogen Bonding, Magnetic Resonance Spectroscopy, Molecular Structure, Protein Binding, Protons
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1390894
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