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

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

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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 D₂O and H ₂O. 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 H₂O and D₂O 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 D₂O compared with H₂O.

Original language	English (US)
Pages (from-to)	15188-15193
Number of pages	6
Journal	Journal of the American Chemical Society
Volume	131
Issue number	42
DOIs	https://doi.org/10.1021/ja9040785
State	Published - Oct 28 2009

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja9040785

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title = "Hydrogen bonding of β-turn structure is stabilized in D2O",

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 D2O and H 2O. 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 H2O and D2O 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 D2O compared with H2O.",

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

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T1 - Hydrogen bonding of β-turn structure is stabilized in D2O

AU - Cho, Younhee

AU - Sagle, Laura B.

AU - Iimura, Satoshi

AU - Zhang, Yanjie

AU - Kherb, Jaibir

AU - Chilkoti, Ashutosh

AU - Scholtz, J. Martin

AU - Cremer, Paul S.

PY - 2009/10/28

Y1 - 2009/10/28

N2 - 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 D2O and H 2O. 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 H2O and D2O 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 D2O compared with H2O.

AB - 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 D2O and H 2O. 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 H2O and D2O 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 D2O compared with H2O.

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 42

ER -

Hydrogen bonding of β-turn structure is stabilized in D₂O

Abstract

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