Arginyl residues and thermal stability in proteins.
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.
D000426:Alcohol Dehydrogenase; D000577:Amides; D001120:Arginine; D055598:Chemical Phenomena; D002621:Chemistry; D004355:Drug Stability; D019791:Guanidine; D006146:Guanidines; D006358:Hot Temperature; D007096:Imidoesters; D008782:Methylurea Compounds; D010751:Phosphopyruvate Hydratase; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012710:Serum Albumin, Bovine
D000577:Amides; D006146:Guanidines; D007096:Imidoesters; D008782:Methylurea Compounds; C002249:O-methylisourea; D012710:Serum Albumin, Bovine; D001120:Arginine; C010222:methyl acetimidate; D000426:Alcohol Dehydrogenase; D010751:Phosphopyruvate Hydratase; D019791:Guanidine