DETERMINATION OF THE STRUCTURE OF A FOLDING NUCLEUS IN BOVINE $\beta$-LACTOGLOBULIN USING UV FLUORESCENCE AND IR/UV DOUBLE RESONANCE SPECTROSCOPY IN THE GAS PHASE}
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Date
2008
Journal Title
Journal ISSN
Volume Title
Publisher
Ohio State University
Abstract
The amino acids in the 19$^{th}$ through 23$^{rd}$ positions of bovine $\beta$-lactoglobulin, Trp-Tyr-Ser-Leu-Ala, have been identified as a folding nucleus} (2002), \textbf{41}, 2786-2796.}, a region of the protein that folds first and may induce or facilitate the proper folding of the remainder of the protein. Thus, the intramolecular interactions in this region of the molecule are of particular interest. Reported here are the structures of Ac-Trp-Tyr-NH$_{2}$, Ac-Trp-Tyr-Ser-NH$_{2}$, and Ac-Trp-Tyr-Ser-Leu-NH$_{2}$ as determined by UV fluorescence and UV/IR double resonance spectroscopy. Shifts in the positions of N-H and O-H bands provide information about hydrogen bonds and $\pi$-electron interactions involving the peptide backbone and/or residues. Predicted structures are then compared with similar peptides and the lowest energy structures determined by \textit{ab initio} calculations to further justify the assignment of the structure.
Description
[2]L. Ragona, M. Catalano, L. Zetta, R. Longhi, F. Fogolari, and H. Molinari. Biochemistry[1]Supported in part by NSF (CHE-0615755)
Author Institution: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260; Laboratoire Francis Perrin, URA 2453 CNRS, Service des Photons, Atomes et Molecules CEA Saclay,Bat 522, 91191 Gif-sur-Yvette Cedex, France
Author Institution: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260; Laboratoire Francis Perrin, URA 2453 CNRS, Service des Photons, Atomes et Molecules CEA Saclay,Bat 522, 91191 Gif-sur-Yvette Cedex, France