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In cytochrome c, the unfolding reaction occurs in four discreet stops, as monitored by the exchange of solvent hydrogen for backbone aminde hydrogens under varying denaturant concentrations.
Direct NMR observation of a transient folding intermediate provides new evidence for the importance of molten globules as general intermediates in protein folding.
Identification of the residues involved in the reaction catalysed by aldehyde reductase should aid in the development of drugs for the treatment of diabetic complications.
Two DNA-RNA chimers, complexed with DNA minor groove binding drugs, have been observed to adopt the B-form conformation for the first time. Thus, the RNA duplex may assume the B-DNA conformation when interacting with drugs, peptides or proteins.
NMR structures of calmodulin, troponin C and related proteins are providing the atomic details of the conformational changes that transduce Ca2+ signals into mechanical or metabolic responses.
The structure of the apo form of calcyclin, a member of the S100 family of calcium-binding proteins, reveals a novel dimer fold that may reflect the presence of a new interface for target protein recognition.