TY - JOUR
T1 - The interaction of tubulin and other proteins with structure-stabilizing solvents
AU - Timasheff, Serge N.
AU - Lee, James C.
AU - Pittz, Eugene P.
AU - Tweedy, Neil
N1 - Funding Information:
This paper was supported by NIH Grants GM-14603 and CA 16707, NSF Grant GB-38544X and a grant from the American Cancer Society, Massachusetts Division.
PY - 1976/6
Y1 - 1976/6
N2 - A study has been carried out of the interactions with proteins of solvent systems which are commonly used to stabilize proteins in solution or to crystallize proteins out of solution. The first class consisted of water-sucrose and water-glycerol, which are frequently added to enzyme solutions in order to maintain their activity; the second class contained sodium and ammonium sulfates and 2-methyl-2,4-pentanediol (MPD) as solvent components. Densimetry and differential refractometry experiments with the application of multicomponent thermodynamic theory, showed that, in all four systems, proteins are preferentially hydrated, i.e., addition of these cosolvents results in an unfavorable free energy change. Detailed analysis of the thermodynamics of protein transitions in the presence of sucrose showed that its stabilizing action can be accounted for to a great extent in terms of the surface energy of this solvent system.
AB - A study has been carried out of the interactions with proteins of solvent systems which are commonly used to stabilize proteins in solution or to crystallize proteins out of solution. The first class consisted of water-sucrose and water-glycerol, which are frequently added to enzyme solutions in order to maintain their activity; the second class contained sodium and ammonium sulfates and 2-methyl-2,4-pentanediol (MPD) as solvent components. Densimetry and differential refractometry experiments with the application of multicomponent thermodynamic theory, showed that, in all four systems, proteins are preferentially hydrated, i.e., addition of these cosolvents results in an unfavorable free energy change. Detailed analysis of the thermodynamics of protein transitions in the presence of sucrose showed that its stabilizing action can be accounted for to a great extent in terms of the surface energy of this solvent system.
UR - http://www.scopus.com/inward/record.url?scp=0000551536&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0000551536&partnerID=8YFLogxK
U2 - 10.1016/0021-9797(76)90076-X
DO - 10.1016/0021-9797(76)90076-X
M3 - Article
AN - SCOPUS:0000551536
SN - 0021-9797
VL - 55
SP - 658
EP - 663
JO - Journal of Colloid And Interface Science
JF - Journal of Colloid And Interface Science
IS - 3
ER -