Native-state energetics of a thermostabilized variant of ribonuclease HI
- 7 December 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 314 (4) , 863-871
- https://doi.org/10.1006/jmbi.2001.5184
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Protein misfolding, evolution and diseasePublished by Elsevier ,1999
- Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and diseaseProceedings of the National Academy of Sciences, 1999
- PATHOLOGIC CONFORMATIONS OF PRION PROTEINSAnnual Review of Biochemistry, 1998
- Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseasesStructure, 1997
- Analysis of the effect of local interactions on protein stabilityFolding and Design, 1996
- .alpha.-Helix stability and the native state of myoglobinBiochemistry, 1993
- An essential proline in .lambda. repressor is required for resistance to intracellular proteolysisBiochemistry, 1990
- Substantial increase of protein stability by multiple disulphide bondsNature, 1989
- The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S‐peptide analogues with enhanced helical stabilityProteins-Structure Function and Bioinformatics, 1986
- Disulfide Bond Engineered into T4 Lysozyme: Stabilization of the Protein Toward Thermal InactivationScience, 1984