The folding kinetics of ribonuclease Sa and a charge-reversal variant
The primary objective was to study the kinetics of folding of RNase Sa. Wild-type RNase Sa does not contain tryptophan. A tryptophan was substituted at residue 81 (WT*) to allow fluorescence spectroscopy to be used to monitor folding. This tryptophan mutation did not change the stability. An analysi...
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| Format: | Others |
| Language: | en_US |
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Texas A&M University
2005
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| Online Access: | http://hdl.handle.net/1969.1/1431 |