Hydrogen Bonding of β-Turn Structure Is Stabilized in D2O

Younhee Cho; Laura B. Sagle; Satoshi Iimura; Yanjie Zhang; Jaibir Kherb; Ashutosh Chilkoti; J. Martin Scholtz; Paul S. Cremer

doi:10.1021/ja9040785

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Hydrogen Bonding of β-Turn Structure Is Stabilized in D2O

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Hydrogen Bonding of β-Turn Structure Is Stabilized in D2O

Younhee Cho, Laura B. Sagle, Satoshi Iimura, Yanjie Zhang, Jaibir Kherb, Ashutosh Chilkoti, J. Martin Scholtz and Paul S. Cremer

Journal of the American Chemical Society, Vol.131(42), pp.15188-15193

10/28/2009

DOI: 10.1021/ja9040785

PMCID: PMC3003597

PMID: 19919159

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https://www.ncbi.nlm.nih.gov/pmc/articles/3003597View

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Abstract

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 β -turn/ β -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.

Details

Title: Subtitle: Hydrogen Bonding of β-Turn Structure Is Stabilized in D2O
Creators: Younhee Cho - Duke University
Laura B. Sagle - Duke University
Satoshi Iimura - Texas A&M Health Science Center
Yanjie Zhang - Texas A&M Health Science Center
Jaibir Kherb - Duke University
Ashutosh Chilkoti - Duke University
J. Martin Scholtz - Texas A&M Health Science Center
Paul S. Cremer - Duke University
Resource Type: Journal article
Publication Details: Journal of the American Chemical Society, Vol.131(42), pp.15188-15193
DOI: 10.1021/ja9040785
PMID: 19919159
PMCID: PMC3003597
NLM abbreviation: J Am Chem Soc
ISSN: 0002-7863
eISSN: 1520-5126
Language: English
Date published: 10/28/2009
Academic Unit: Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
Record Identifier: 9984288722802771

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