Abstract
Temperature-jump circular dichroism, a new relaxation technique, has been used to study the interaction of liver alcohol dehydrogenase with the chromophoric inhibitor, auramine 0. While a single relaxation, τ = 250 μs, is observed in transmission parameters, the simultaneous observation of transient CD indicates two processes, τ1 < 300 μs and τ2 = 200 ms. The slower process is interpreted as a relaxation between two conformational states of the enzyme-inhibitor complex which are present in solution. These differ substantially in their symmetry properties. Temperature-jump circular dichroism provides information on rates of conformational changes in biomolecular structures which is not accessible by other spectroscopic methods.
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