Title : [Comparison of Physico-chemical Aspects between E. coli and Human Dihydrofolate Reductase: an Equilibrium Unfolding Study].

Pub. Date : 2015 May-Jun

PMID : 26349210






1 Functional Relationships(s)
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1 The equilibrium unfolding mechanism of dihydrofolate reductase proteins using guanidine hydrochloride as a denaturant in the presence of various types of osmolytes has been monitored using loss in enzymatic activity, intrinsic tryptophan fluorescence and an extrinsic fluorophore 8-anilino-1-naphthalene-sulfonic acid as probes. 8-anilino-1-naphthalenesulfonic acid dihydrofolate reductase Homo sapiens