Skip to main content
Journal cover image

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

Publication ,  Journal Article
Cho, Y; Sagle, LB; Iimura, S; Zhang, Y; Kherb, J; Chilkoti, A; Scholtz, JM; Cremer, PS
Published in: Journal of the American Chemical Society
October 2009

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.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Journal of the American Chemical Society

DOI

EISSN

1520-5126

ISSN

0002-7863

Publication Date

October 2009

Volume

131

Issue

42

Start / End Page

15188 / 15193

Related Subject Headings

  • Temperature
  • Protein Structure, Secondary
  • Peptides
  • Models, Molecular
  • Hydrophobic and Hydrophilic Interactions
  • Hydrogen Bonding
  • General Chemistry
  • Elastin
  • Deuterium Oxide
  • Circular Dichroism
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Cho, Y., Sagle, L. B., Iimura, S., Zhang, Y., Kherb, J., Chilkoti, A., … Cremer, P. S. (2009). Hydrogen bonding of beta-turn structure is stabilized in D(2)O. Journal of the American Chemical Society, 131(42), 15188–15193. https://doi.org/10.1021/ja9040785
Cho, Younhee, Laura B. Sagle, Satoshi Iimura, Yanjie Zhang, Jaibir Kherb, Ashutosh Chilkoti, J Martin Scholtz, and Paul S. Cremer. “Hydrogen bonding of beta-turn structure is stabilized in D(2)O.Journal of the American Chemical Society 131, no. 42 (October 2009): 15188–93. https://doi.org/10.1021/ja9040785.
Cho Y, Sagle LB, Iimura S, Zhang Y, Kherb J, Chilkoti A, et al. Hydrogen bonding of beta-turn structure is stabilized in D(2)O. Journal of the American Chemical Society. 2009 Oct;131(42):15188–93.
Cho, Younhee, et al. “Hydrogen bonding of beta-turn structure is stabilized in D(2)O.Journal of the American Chemical Society, vol. 131, no. 42, Oct. 2009, pp. 15188–93. Epmc, doi:10.1021/ja9040785.
Cho Y, Sagle LB, Iimura S, Zhang Y, Kherb J, Chilkoti A, Scholtz JM, Cremer PS. Hydrogen bonding of beta-turn structure is stabilized in D(2)O. Journal of the American Chemical Society. 2009 Oct;131(42):15188–15193.
Journal cover image

Published In

Journal of the American Chemical Society

DOI

EISSN

1520-5126

ISSN

0002-7863

Publication Date

October 2009

Volume

131

Issue

42

Start / End Page

15188 / 15193

Related Subject Headings

  • Temperature
  • Protein Structure, Secondary
  • Peptides
  • Models, Molecular
  • Hydrophobic and Hydrophilic Interactions
  • Hydrogen Bonding
  • General Chemistry
  • Elastin
  • Deuterium Oxide
  • Circular Dichroism