Hydrogen bonding of beta-turn structure is stabilized in D(2)O.

Journal Article (Journal Article)

The lower critical solution temperature (LCST) of elastin-like polypeptides (ELPs) was investigated as a function of ELP chain length and guest residue chemistry. These measurements were made in both D(2)O and H(2)O. Differences in the LCST values with heavy and light water were correlated with secondary structure formation of the polypeptide chains. Such structural information was obtained by circular dichroism and infrared measurements. Additional thermodynamic data were obtained by differential scanning calorimetry. It was found that there is a greater change in the LCST value between H(2)O and D(2)O for those polypeptides which form the greatest amount of beta-turn/beta-aggregate structure. Moreover, these same molecules were the least hydrophobic ELPs. Therefore, hydrogen bonding rather than hydrophobicity was the key factor in the stabilization of the collapsed state of ELPs in D(2)O compared with H(2)O.

Full Text

Duke Authors

Cited Authors

  • Cho, Y; Sagle, LB; Iimura, S; Zhang, Y; Kherb, J; Chilkoti, A; Scholtz, JM; Cremer, PS

Published Date

  • October 2009

Published In

Volume / Issue

  • 131 / 42

Start / End Page

  • 15188 - 15193

PubMed ID

  • 19919159

Pubmed Central ID

  • PMC3003597

Electronic International Standard Serial Number (EISSN)

  • 1520-5126

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja9040785


  • eng