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The method utilizes side chain rotamer library and tests whether any of the common rotamers can be fitted into the protein structure. We present an analysis of the role of cysteine reactivity as a regulatory factor in proteins, emphasizing the interplay between electrostatics and redox potential as key determinants of the resulting oxidation state. As expected, the mutant (f370c), where phenylalanine had been replaced by cysteine at a homologous position, showed reduced sensitivity to tea (fig

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5b) when compared with the wild,. The notable features of this method include its tolerance of steric hinderance from the side groups on either ligating terminus, thereby allowing flexible disconnection at sites that are otherwise difficult to functionalize. Probably the best known example of this occurs within the cysteine proteases, such as caspases or papains, where cysteine is the key catalytic residue, being helped by a histidine and an asparagine.

Our experiments demonstrate that the sers spectra are sensitive to chirality of interacting cysteine and phenylalanine molecules at the silver electrode surface, thus indicating the possibility of using this method for enantiomeric recognition of amino acids.

Here, we present a quantitative approach of identifying steric clashes in proteins by defining clashes based on the van der waals repulsion energy of the clashing atoms. In this study we have determined whether cysteine substitution mutations of equivalent residues in p2x 2 and p2x 4 receptors have similar effects and if these mutant receptors can be regulated by charged methanethiosulfonate (mts) compounds.