Conformational stability, flexibility, and steady-state activity of Ribonuclease T1 variants /
(Shirley et al., 1992; Thomson et al., 1989). We observe a
| Main Author: | |
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1995.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | (Shirley et al., 1992; Thomson et al., 1989). We observe a and the determined Kcat/Km values. With the exception of conformational dynamics. The mutants can be classified into decreased activity from wild-type values; those with decreased stability and decreased activity; and those with decreased stability and increased activity. The fourth dependence of mutational effects. Although results are determined at pH 7.0 and 25 'C. These mutants comprise a 4 for binding and catalysis. Variation in activity among kcal/mol range in global stability under similar conditions mutants of similar stability demonstrates the context observed, possibly due to decreases in flexibility required possibility, increased stability and activity was not preliminary, this model system may reflect a universal relationship between stability and activity. relationship between the variants' conformational stability The steady-state kinetic parameters for GpC hydrolysis by three categories: those with increased stability and three mutations made to the active site, differences from wild-type activity are believed to be a result of changes in wild-type RNase T1 and 14 single-residue mutants were |
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| Item Description: | "Major subject: Chemistry". Vita. |
| Physical Description: | viii, 59 leaves : illustrations ; 28 cm. Also available online. Issued also on microfiche from Lange Micrographics. |
| Bibliography: | Includes bibliographical references. |