Effects of cation-pi interactions on the stability of the alpha helix

ORGN 496

Alison McCurdy, Rex Cheng, and Ronald W. Tan. Department of Chemistry and Biochemistry, CSU Los Angeles, 5151 State University Dr, Los Angeles, CA 90032
Understanding the subtleties in protein structure and stability is important in many biochemical and medical applications. Specifically, side chain interactions have been found to play a role in the stability of α-helices. The nature of side chain interactions between aromatic residues and cations is not yet fully characterized. This cation-pi interaction has been documented in both artificial and natural systems. In this work, the strength of two cation-pi interactions (trp-arg, tyr-lys) in an alanine-based model helix will be assessed using circular dichroism (CD). Relative stabilities of peptides with residues spaced (i, i+4) and (i, i+5) will be determined using thermal and denaturant unfolding curves.
 

Total Synthesis, Asymmetric Reactions and Syntheses, Bioorganic
9:00 AM-11:00 AM, Wednesday, March 31, 2004 Anaheim Convention Center -- Hall C, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, March 29, 2004 Anaheim Convention Center -- Hall A, Sci-Mix

Division of Organic Chemistry

The 227th ACS National Meeting, Anaheim, CA, March 28-April 1, 2004