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The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed-disulfide intermediate between thioredoxin and the substrate. In order to model the interaction, we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue. A specific covalent complex has been prepared between the remaining cysteine residue and a short cysteine-containing peptide. This paper describes the preparation and characterization of the mutant protein both free and in the peptide complex. [ABSTRACT FROM AUTHOR]

Examines the effects of chain length on the propensity of short peptides to form helix-like structures in aqueous solution. Contribution of increased length and intact capping sequences; Evidence for the formation of a significant population of helical conformers; Existence of correlation between the amide prton chemical shift and temperature coefficient.

Examines the structural basis for the activity of retro-Diels-Alder catalytic antibodies. Paradigm for designing catalytic antibodies; Factor contributing to the reactivity of regioisomers; Hydrogen-bonding interactions between the nitroxyl bridge and the backbone amide of water molecule.