ORGN 698 |
| John T. Gerig, Department of Chemistry and Biochemistry, Department of Chemistry and Biochemistry, University of California, Santa Barbara, Mail Code 9510, Santa Barbara, CA 93106 |
| Nuclear Overhauser effects arising from the interactions of spins of solvent molecules with spins of a solute should reveal the “exposure” of solute spins to collisions with solvent. A computational method for predicting these effects will be described along with experimental results from model systems which indicate the reliability of the predictions so made. Application of these approaches to examination of the interactions between the peptide melittin and the solvent components of 35% hexafluoroisopropanol/ water will be described. Standard NOESY experiments indicate that the structure of this peptide consists of two a-helical regions separated by a bend between Thr10 and Ala15. Intermolecular 1H{19F} solute-solvent NOEs are generally consistent with this structure except in the region of the bend where interactions between the peptide and fluoroalcohol appear to be much stronger than expected. Intermolecular 1H{1H} solute-solvent NOEs indicate little interaction with water of the solvent mixture except in the region of the bend. (Supported by the Petroleum Research Fund.) |
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Proteins, Peptides, Amino Acids, and Nucleotides
8:30 AM-11:30 AM, Thursday, September 11, 2003 Sheraton New York -- Royal Ballroom B, Oral
Division of Organic Chemistry |