A kinetic study of the folding of nuclease B, a possible precursor of staphylococcal nuclease A.
Nuclease B, which contains an additional flexible amino acid sequence of 19 amino acid residues bound to the NH2-terminus of nuclease A, an extracellular nuclease of Staphylococcus aureus, has been investigated in order to determine the influence of the extra residues on the refolding of the nuclease A portion from the acid denaturated state by monitoring the change in tryptophan fluorescence using a stopped-flow technique. It was found that the kinetic parameters of this refolding is similar within experimental error for nuclease A and nuclease B for the entire course (up to 40 s) studied. Therefore, the extra residues do not appear to have any detectable effect on the dynamic events involved in the refolding process. Thus, the folding of the nuclease A portion of nuclease B appears to be thermodynamically and kinetically independent of the 19 residues at the amino-terminus.
D000595:Amino Acid Sequence; D003851:Deoxyribonucleases / Q000378:metabolism*; D007700:Kinetics; D011487:Protein Conformation; D011489:Protein Denaturation; D012260:Ribonucleases / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013211:Staphylococcus aureus / Q000201:enzymology*
D003851:Deoxyribonucleases; D012260:Ribonucleases