Arginyl residues and thermal stability in proteins.
F S Qaw, J M Brewer
Index: Mol. Cell Biochem. 71(2) , 121-7, (1986)
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Abstract
Guanidination and amidination of bovine serum albumin, yeast enolase and yeast alcohol dehydrogenase were accompanied by increases in thermal stability at lower extents of modification. Decreases in thermal stability result from greater modification. These results support suggestions that surface guanidino groups (arginyl groups) are an important factor in thermal stability of proteins.
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