"Glass transition" in peptides: Temperature and pressure effects

P. Papadopoulos; G. Floudas; I. Schnell; H. A. Klok; T. Aliferis; H. Iatrou; N. Hadjichristidis

doi:10.1063/1.1931657

"Glass transition" in peptides: Temperature and pressure effects

P. Papadopoulos^*, G. Floudas, I. Schnell, H. A. Klok, T. Aliferis, H. Iatrou, N. Hadjichristidis

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

33 Scopus citations

Abstract

We report on the origin of the liquid-to-glass transition in a series of oligopeptides of γ -benzyl- L -glutamate up to the polymer (PBLG), and in Poly- Z - L -lysine (PZLL) and Polyglycine (PGly) using dielectric spectroscopy as a function of temperature and pressure. We show that temperature is the dominant control variable of the dynamics associated with the peptidic "glass transition." This is an intrinsic feature of the peptide dynamics, irrespective of the type of amino acid and of the peptide secondary structure. The influence of the type of secondary structure (α helix vs Β sheet) on the liquid-to-glass dynamics is discussed.

Original language	English (US)
Article number	224906
Journal	JOURNAL OF CHEMICAL PHYSICS
Volume	122
Issue number	22
DOIs	https://doi.org/10.1063/1.1931657
State	Published - Jun 8 2005
Externally published	Yes

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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title = "{"}Glass transition{"} in peptides: Temperature and pressure effects",

abstract = "We report on the origin of the liquid-to-glass transition in a series of oligopeptides of γ -benzyl- L -glutamate up to the polymer (PBLG), and in Poly- Z - L -lysine (PZLL) and Polyglycine (PGly) using dielectric spectroscopy as a function of temperature and pressure. We show that temperature is the dominant control variable of the dynamics associated with the peptidic {"}glass transition.{"} This is an intrinsic feature of the peptide dynamics, irrespective of the type of amino acid and of the peptide secondary structure. The influence of the type of secondary structure (α helix vs Β sheet) on the liquid-to-glass dynamics is discussed.",

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T2 - Temperature and pressure effects

AU - Papadopoulos, P.

AU - Floudas, G.

AU - Schnell, I.

AU - Klok, H. A.

AU - Aliferis, T.

AU - Iatrou, H.

AU - Hadjichristidis, N.

PY - 2005/6/8

Y1 - 2005/6/8

N2 - We report on the origin of the liquid-to-glass transition in a series of oligopeptides of γ -benzyl- L -glutamate up to the polymer (PBLG), and in Poly- Z - L -lysine (PZLL) and Polyglycine (PGly) using dielectric spectroscopy as a function of temperature and pressure. We show that temperature is the dominant control variable of the dynamics associated with the peptidic "glass transition." This is an intrinsic feature of the peptide dynamics, irrespective of the type of amino acid and of the peptide secondary structure. The influence of the type of secondary structure (α helix vs Β sheet) on the liquid-to-glass dynamics is discussed.

AB - We report on the origin of the liquid-to-glass transition in a series of oligopeptides of γ -benzyl- L -glutamate up to the polymer (PBLG), and in Poly- Z - L -lysine (PZLL) and Polyglycine (PGly) using dielectric spectroscopy as a function of temperature and pressure. We show that temperature is the dominant control variable of the dynamics associated with the peptidic "glass transition." This is an intrinsic feature of the peptide dynamics, irrespective of the type of amino acid and of the peptide secondary structure. The influence of the type of secondary structure (α helix vs Β sheet) on the liquid-to-glass dynamics is discussed.

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DO - 10.1063/1.1931657

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"Glass transition" in peptides: Temperature and pressure effects

Abstract

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