Protein dynamics in viscous solvents

G. Caliskan; A. Kisliuk; A. M. Tsai; C. L. Soles; A. P. Sokolov

doi:10.1063/1.1541614

Protein dynamics in viscous solvents

G. Caliskan, A. Kisliuk, A. M. Tsai, C. L. Soles, A. P. Sokolov

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62 Scopus citations

Abstract

Low-frequency Raman spectroscopy was used to directly probe the dynamical differences of the protein lysozyme preserved in both glycerol and trehalose. Strong differences were identified in the manner by which glycerol and trehalose affect the picosecond dynamics of lysozyme over a wide range of temperatures. These differences correlate strongly with established trends in the biochemical activity and denaturation temperatures.

Original language	English
Pages (from-to)	4230-4236
Number of pages	7
Journal	Journal of Chemical Physics
Volume	118
Issue number	9
DOIs	https://doi.org/10.1063/1.1541614
State	Published - Mar 1 2003
Externally published	Yes

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10.1063/1.1541614

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title = "Protein dynamics in viscous solvents",

abstract = "Low-frequency Raman spectroscopy was used to directly probe the dynamical differences of the protein lysozyme preserved in both glycerol and trehalose. Strong differences were identified in the manner by which glycerol and trehalose affect the picosecond dynamics of lysozyme over a wide range of temperatures. These differences correlate strongly with established trends in the biochemical activity and denaturation temperatures.",

author = "G. Caliskan and A. Kisliuk and Tsai, {A. M.} and Soles, {C. L.} and Sokolov, {A. P.}",

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AU - Caliskan, G.

AU - Kisliuk, A.

AU - Tsai, A. M.

AU - Soles, C. L.

AU - Sokolov, A. P.

PY - 2003/3/1

Y1 - 2003/3/1

N2 - Low-frequency Raman spectroscopy was used to directly probe the dynamical differences of the protein lysozyme preserved in both glycerol and trehalose. Strong differences were identified in the manner by which glycerol and trehalose affect the picosecond dynamics of lysozyme over a wide range of temperatures. These differences correlate strongly with established trends in the biochemical activity and denaturation temperatures.

AB - Low-frequency Raman spectroscopy was used to directly probe the dynamical differences of the protein lysozyme preserved in both glycerol and trehalose. Strong differences were identified in the manner by which glycerol and trehalose affect the picosecond dynamics of lysozyme over a wide range of temperatures. These differences correlate strongly with established trends in the biochemical activity and denaturation temperatures.

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U2 - 10.1063/1.1541614

DO - 10.1063/1.1541614

M3 - Article

AN - SCOPUS:0037338828

SN - 0021-9606

VL - 118

SP - 4230

EP - 4236

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

IS - 9

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Protein dynamics in viscous solvents

Abstract

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