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Effects of sugars on the thermal stability of a protein
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10.1063/1.4811287
/content/aip/journal/jcp/138/24/10.1063/1.4811287
http://aip.metastore.ingenta.com/content/aip/journal/jcp/138/24/10.1063/1.4811287

Figures

Image of FIG. 1.
FIG. 1.

Close packing of side chains of a protein and protein-solvent contact. The overlap of excluded volumes leads to an increase in the total volume available to the translational displacement of solvent molecules. The contact of a solvent molecule with the protein also induces the overlap of excluded volumes generated by the protein and the solvent molecule, which causes a larger translational restriction for the contacting solvent molecule but brings an increase in the total volume available to the translational displacement of the other solvent molecules (see the third paragraph in Sec. IV D ).

Image of FIG. 2.
FIG. 2.

(a) Physical picture of thermal denaturation for different proteins in water with no sugar added. Three proteins, “a,” “b,” and “c,” are considered. Δ and Δ are the solvent-entropy gain and the conformational-entropy loss upon protein folding, respectively. is the denaturation temperature. The subscripts, “a,” “b,” and “c,” denote the values for proteins “a,” “b,” and “c,” respectively. The minimum value of the abscissa is 298 K. (b) Physical picture of thermal denaturation for a protein in different solvents. Three solvents, “α,” “β,” and “γ,” are considered. Δ is the solvent-entropy gain in each solvent upon protein folding. The subscripts, “α,” “β,” and “γ,” denote the values for solvents “α,” “β,” and “γ,” respectively.

Image of FIG. 3.
FIG. 3.

Dependence of the criterion of the thermal stability on sugar species, sucrose (square) and glucose (circle), and sugar concentration.

Tables

Generic image for table
Table I.

Denaturation temperatures and measures of the thermal stability Δ /( ) and Δ /( ) for Yfh1, CyaY, and hfra. The superscript “w” represents that the solvent-entropy gain upon protein folding is calculated for water with no sugar added, and the superscripts “mp” and “hs” represent that the multipolar-model water and the hard-sphere solvent are employed for water, respectively. The number density and molecular diameter are set at those of real water.

Generic image for table
Table II.

Physical origins and signs of the four constituents of the solvation entropy for water with no sugar added.

Generic image for table
Table III.

Change in the solvent-entropy gain upon protein folding caused by sugar addition and its constituents. They are scaled by the Boltzmann constant .

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/content/aip/journal/jcp/138/24/10.1063/1.4811287
2013-06-25
2014-04-18
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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Effects of sugars on the thermal stability of a protein
http://aip.metastore.ingenta.com/content/aip/journal/jcp/138/24/10.1063/1.4811287
10.1063/1.4811287
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