| dc.contributor.advisor | Pace, C. N. | |
| dc.creator | Erickson, Rick | |
| dc.date.accessioned | 2022-04-01T16:03:53Z | |
| dc.date.available | 2022-04-01T16:03:53Z | |
| dc.date.issued | 1990 | |
| dc.identifier.uri | https://hdl.handle.net/1969.1/CAPSTONE-NormanB_1977 | |
| dc.description | Program year: 1989/1990 | en |
| dc.description | Digitized from print original stored in HDR | en |
| dc.description.abstract | The Asp15-->Ala mutant of ribonuclease T1 (RNase T1) was constructed by site-directed mutagenesis, cloned and expressed in Escherichia coli. This mutant was synthesized to determine whether or not the aspartic acid at position 15 is a cation binding site as predicted by x-ray crystallography. The conformational stability of the mutant's folded state increased by 0.97 kcal/mol in 0.15M NaCl and by 1.33 kcal/mol in 0.20M CaCl2. These results indicate that cations are still being bound by the mutant. This means that our previous thoughts on the contribution of the cation binding site to the stability of RNase T1 were not correct and that further studies are needed. | en |
| dc.format.extent | 29 pages | en |
| dc.format.medium | electronic | en |
| dc.format.mimetype | application/pdf | |
| dc.subject | Escherichia coli | en |
| dc.subject | stability | en |
| dc.subject | cation binding site | en |
| dc.subject | cations | en |
| dc.title | Cation Binding and the Conformational Stability of Ribonuclease T1 | en |
| dc.type | Thesis | en |
| thesis.degree.department | Biochemistry | en |
| thesis.degree.grantor | University Undergraduate Fellow | en |
| thesis.degree.level | Undergraduate | en |
| dc.type.material | text | en |
