| Literature DB >> 14163781 |
Abstract
The effects of various neutral salts on the temperature of the thermally-induced denaturation of the globular protein ribonuclease are described and compared with the effects of these salts on helix-coil transition temperatures in other macromolecules. These agents affect the stability of the native form of macromolecules as diverse as ribonuclease, collagen, DNA, and myosin in very similar ways; salts such as KSCN and CaCl(2) serve as very potent general structural destabilizers or denaturants, while salts such as (NH(4))(2)SO(4) and K(2)HPO(4) strongly stabilize the native conformation. The effectiveness of the neutral salts as ribonuclease destabilizers is compared with that of urea and the guanidinium salts.Entities:
Keywords: ACETATES; AMMONIUM COMPOUNDS; BENZOATES; BROMIDES; CALCIUM; CHEMISTRY; CHLORIDES; COLLAGEN; DNA; EXPERIMENTAL LAB STUDY; GELATIN; IODIDES; LITHIUM; MUSCLE PROTEINS; NITRATES; PERCHLORIC ACIDS; PHOSPHATES; POTASSIUM; REVIEW; RIBONUCLEASE; SALTS; SODIUM; SULFATES; THIOCYANATES
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Year: 1964 PMID： 14163781 DOI： 10.1126/science.145.3632.577
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728