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Biologically significant conformation of the Saccharomyces cerevisiae α-factor

✍ Scribed by Fred Naider; Linda A. Jelicks; Jeffrey M. Becker; Michelle S. Broido

Publisher
Wiley (John Wiley & Sons)
Year
1989
Tongue
English
Weight
539 KB
Volume
28
Category
Article
ISSN
0006-3525

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✦ Synopsis

The conformation of the tridecapeptide a-factor of the yeast Saccharomyces cerewisiue was examined in both solution and in the presence of lipid vesicles. CD, differential scanning calorimetry, and phoephonu, nmr all indicate that this mating pheromone interacts with lipid vesicles. In both aqueous and organic solution the a-factor is a flexible molecule that exhibits features of a type I1 8-tm spanning the center of the peptide. Two-dimensional Nuclear Overhauser enhancement spectroscopy gives evidence that the 8-tum is stabilized on interaction of the peptide with lipid vesicles. Our current belief is that the P -t m may play an important role in the biologically active conformation of the a-factor.

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