The stabilization of proteins by sucrose.

James Lee, S. N. Timasheff

Research output: Contribution to journalArticle

924 Citations (Scopus)

Abstract

The interactions between proteins and solvent components have been investigated for the sucrose/water system. Thermodynamic and kinetic measurements of the thermal unfolding of alpha-chymotrypsin, chymotrypsinogen, and ribonuclease were performed as a function of sucrose concentration. The alteration in protein-solvent interactions in the presence of sucrose was also studied by density measurements and analyzed by multicomponent thermodynamic theory. Sucrose does not induce a conformational change in three proteins studied, although it does induce a small change in the circular dichroism spectrum of ribonuclease. The enthalpy of thermal unfolding shows little dependence on the concentration of sucrose, while the apparent activation energy of the unfolding process is increased by the addition of sucrose. The results from the protein-solvent interaction study indicate that sucrose is preferentially excluded from the protein domain, increasing the free energy of the system. Thermodynamically this leads to protein stabilization since the unfolded state of the protein becomes thermodynamically even less favorable in the presence of sucrose. The exclusion of sucrose from the protein domain seems to be related to the higher cohesive force of the sucrose water solvent system since all the experimental observations can be correlated with the effect of sucrose on the surface tension of water.

Original languageEnglish (US)
Pages (from-to)7193-7201
Number of pages9
JournalJournal of Biological Chemistry
Volume256
Issue number14
StatePublished - Jul 25 1981
Externally publishedYes

Fingerprint

Sucrose
Stabilization
Proteins
Ribonucleases
Thermodynamics
Water
Hot Temperature
Chymotrypsinogen
Protein Unfolding
Surface Tension
Circular Dichroism
Free energy
Surface tension
Enthalpy
Activation energy
Kinetics

ASJC Scopus subject areas

  • Biochemistry

Cite this

Lee, J., & Timasheff, S. N. (1981). The stabilization of proteins by sucrose. Journal of Biological Chemistry, 256(14), 7193-7201.

The stabilization of proteins by sucrose. / Lee, James; Timasheff, S. N.

In: Journal of Biological Chemistry, Vol. 256, No. 14, 25.07.1981, p. 7193-7201.

Research output: Contribution to journalArticle

Lee, J & Timasheff, SN 1981, 'The stabilization of proteins by sucrose.', Journal of Biological Chemistry, vol. 256, no. 14, pp. 7193-7201.
Lee J, Timasheff SN. The stabilization of proteins by sucrose. Journal of Biological Chemistry. 1981 Jul 25;256(14):7193-7201.
Lee, James ; Timasheff, S. N. / The stabilization of proteins by sucrose. In: Journal of Biological Chemistry. 1981 ; Vol. 256, No. 14. pp. 7193-7201.
@article{940b84fd87664ef0a41ae2f262d94325,
title = "The stabilization of proteins by sucrose.",
abstract = "The interactions between proteins and solvent components have been investigated for the sucrose/water system. Thermodynamic and kinetic measurements of the thermal unfolding of alpha-chymotrypsin, chymotrypsinogen, and ribonuclease were performed as a function of sucrose concentration. The alteration in protein-solvent interactions in the presence of sucrose was also studied by density measurements and analyzed by multicomponent thermodynamic theory. Sucrose does not induce a conformational change in three proteins studied, although it does induce a small change in the circular dichroism spectrum of ribonuclease. The enthalpy of thermal unfolding shows little dependence on the concentration of sucrose, while the apparent activation energy of the unfolding process is increased by the addition of sucrose. The results from the protein-solvent interaction study indicate that sucrose is preferentially excluded from the protein domain, increasing the free energy of the system. Thermodynamically this leads to protein stabilization since the unfolded state of the protein becomes thermodynamically even less favorable in the presence of sucrose. The exclusion of sucrose from the protein domain seems to be related to the higher cohesive force of the sucrose water solvent system since all the experimental observations can be correlated with the effect of sucrose on the surface tension of water.",
author = "James Lee and Timasheff, {S. N.}",
year = "1981",
month = "7",
day = "25",
language = "English (US)",
volume = "256",
pages = "7193--7201",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "14",

}

TY - JOUR

T1 - The stabilization of proteins by sucrose.

AU - Lee, James

AU - Timasheff, S. N.

PY - 1981/7/25

Y1 - 1981/7/25

N2 - The interactions between proteins and solvent components have been investigated for the sucrose/water system. Thermodynamic and kinetic measurements of the thermal unfolding of alpha-chymotrypsin, chymotrypsinogen, and ribonuclease were performed as a function of sucrose concentration. The alteration in protein-solvent interactions in the presence of sucrose was also studied by density measurements and analyzed by multicomponent thermodynamic theory. Sucrose does not induce a conformational change in three proteins studied, although it does induce a small change in the circular dichroism spectrum of ribonuclease. The enthalpy of thermal unfolding shows little dependence on the concentration of sucrose, while the apparent activation energy of the unfolding process is increased by the addition of sucrose. The results from the protein-solvent interaction study indicate that sucrose is preferentially excluded from the protein domain, increasing the free energy of the system. Thermodynamically this leads to protein stabilization since the unfolded state of the protein becomes thermodynamically even less favorable in the presence of sucrose. The exclusion of sucrose from the protein domain seems to be related to the higher cohesive force of the sucrose water solvent system since all the experimental observations can be correlated with the effect of sucrose on the surface tension of water.

AB - The interactions between proteins and solvent components have been investigated for the sucrose/water system. Thermodynamic and kinetic measurements of the thermal unfolding of alpha-chymotrypsin, chymotrypsinogen, and ribonuclease were performed as a function of sucrose concentration. The alteration in protein-solvent interactions in the presence of sucrose was also studied by density measurements and analyzed by multicomponent thermodynamic theory. Sucrose does not induce a conformational change in three proteins studied, although it does induce a small change in the circular dichroism spectrum of ribonuclease. The enthalpy of thermal unfolding shows little dependence on the concentration of sucrose, while the apparent activation energy of the unfolding process is increased by the addition of sucrose. The results from the protein-solvent interaction study indicate that sucrose is preferentially excluded from the protein domain, increasing the free energy of the system. Thermodynamically this leads to protein stabilization since the unfolded state of the protein becomes thermodynamically even less favorable in the presence of sucrose. The exclusion of sucrose from the protein domain seems to be related to the higher cohesive force of the sucrose water solvent system since all the experimental observations can be correlated with the effect of sucrose on the surface tension of water.

UR - http://www.scopus.com/inward/record.url?scp=0019888281&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019888281&partnerID=8YFLogxK

M3 - Article

C2 - 7251592

AN - SCOPUS:0019888281

VL - 256

SP - 7193

EP - 7201

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -