TY  - JOUR
ID  - pittir17215
UR  - http://d-scholarship-dev.library.pitt.edu/17215/
IS  - 30
A1  - Ahmed, Z
A1  - Asher, SA
Y1  - 2006/08/01/
N2  - We used UVRRS at 194 and 204 nm excitation to examine the backbone conformation of a 13-residue polypeptide (gp41659-671) that has been shown by NMR to predominantly fold into a 310-helix. Examination of the conformation sensitive AmIII3 region indicates the peptide has significant populations of ?-turn, PPII, 310-helix, and ?-helix-like conformations but little ?-helix. We estimate that at 1 °C on average six of the 12 peptide bonds are in folded conformations (predominantly 310- and ?-helix), while the other six are in unfolded (?-turn/PPII) conformations. The folded and unfolded populations do not change significantly as the temperature is increased from 1 to 60 °C, suggesting a unique energy landscape where the folded and unfolded conformations are essentially degenerate in energy and exhibit identical temperature dependences. © 2006 American Chemical Society.
JF  - Biochemistry
VL  - 45
SN  - 0006-2960
TI  - UV resonance Raman investigation of a 3<inf>10</inf>-helical peptide reveals a rough energy landscape
SP  - 9068 
AV  - public
EP  -  9073
ER  -