Agents chaotropic

Folded proteins can be caused to spontaneously unfold upon being exposed to chaotropic agents, such as urea or guanidine hydrochloride (Gdn), or to elevated temperature (thermal denaturation). As solution conditions are changed by addition of denaturant, the mole fraction of denatured protein increases from a minimum of zero to a maximum of 1.0 in a characteristic unfolding isotherm (Fig. 7a). From a plot such as Figure 7a one can determine the concentration of denaturant, or the temperature in the case of thermal denaturation, required to achieve half maximal unfolding, ie, where... 

Disulfide reduction occurs over a broad pH range and in a variety of buffer environments. The reaction can be done in denaturants, chaotropic agents, detergents, and in high salt conditions. 

METABOLIC CHANNELING CHAOTROPIC AGENTS HOFMEISTER SERIES KOSMOTROPES... 

HOFMEISTER SERIES CHAOTROPIC AGENTS KOSMOTROPES Hofstee plot,... 

COOPERATIVITY ALLOSTERISM INDUCED FIT MODEL MONOD-WYMAN-CHANGEUX MODEL INDEPENDENT BINDING LINKED FUNCTIONS ADAIR EQUATION POSITIVE COOPERATIVITY NEGATIVE COOPERATIVITY KOSMOTROPES CHAOTROPIC AGENTS HOFMEISTER SERIES Kp, Kq, K .. . ... 

These particulate, and also many apparently soluble, DPO enzyme preparations frequently exhibit the phenomenon of latency. This is manifested as atypically low DPO activity when the tissue is known to be rich in DPOs. When the enzyme is treated with a chaotropic agent such as SDS or 8 M urea, or is subjected to an acetone-precipitation procedure, a marked increase in DPO activity is revealed (Palmer, 1963 Walker and Hulme, 1965). This effect is thought to come about by the release of the membrane-bound enzyme and/or effects upon the tertiary structure of the enzyme and the active site. 

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