« Previous Abstract"Conventional water bath heating on undried brewer's spent grain: Functionality, fatty acids, volatiles, polyphenolic and antioxidant properties"    Next AbstractThe alpha-factor mating pheromone of Saccharomyces cerevisiae: a model for studying the interaction of peptide hormones and G protein-coupled receptors »

Biopolymers

Title:		Biologically significant conformation of the Saccharomyces cerevisiae alpha-factor
Author(s):		Naider F; Jelicks LA; Becker JM; Broido MS;
Address:
Journal Title:		Biopolymers
Year:		1989
Volume:		28
Issue:		1
Page Number:		487 - 497
DOI:		10.1002/bip.360280143
ISSN/ISBN:		0006-3525 (Print) 0006-3525 (Linking)
Abstract:		"The conformation of the tridecapeptide alpha-factor of the yeast Saccharomyces cerevisiae was examined in both solution and in the presence of lipid vesicles. CD, differential scanning calorimetry, and phosphorus nmr all indicate that this mating pheromone interacts with lipid vesicles. In both aqueous and organic solution the alpha-factor is a flexible molecule that exhibits features of a type II beta-turn spanning the center of the peptide. Two-dimensional Nuclear Overhauser enhancement spectroscopy gives evidence that the beta-turn is stabilized on interaction of the peptide with lipid vesicles. Our current belief is that the beta-turn may play an important role in the biologically active conformation of the alpha-factor"
Keywords:		"Mating Factor Models, Molecular *Peptides/chemical synthesis *Pheromones Protein Conformation Saccharomyces cerevisiae Structure-Activity Relationship;"
Notes:		"MedlineNaider, F Jelicks, L A Becker, J M Broido, M S eng GM 22086/GM/NIGMS NIH HHS/ GM 22087/GM/NIGMS NIH HHS/ RR-03037/RR/NCRR NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1989/01/01 Biopolymers. 1989 Jan; 28(1):487-97. doi: 10.1002/bip.360280143"