Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate
- 1 March 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 306 (4) , 877-888
- https://doi.org/10.1006/jmbi.2001.4436
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Protein folding: from the levinthal paradox to structure predictionJournal of Molecular Biology, 1999
- Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic powerProtein Engineering, Design and Selection, 1999
- Increasing protein stability by altering long‐range coulombic interactionsProtein Science, 1999
- Protein stability: still an unsolved problemCellular and Molecular Life Sciences, 1997
- Forces contributing to the conformational stability of proteinsThe FASEB Journal, 1996
- Design and structural analysis of an engineered thermostable chicken lysozymeProtein Science, 1995
- Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additiveProtein Engineering, Design and Selection, 1995
- Principles of protein stability derived from protein engineering experimentsCurrent Opinion in Structural Biology, 1993
- Substantial increase of protein stability by multiple disulphide bondsNature, 1989
- Enhanced protein thermostability from designed mutations that interact with α-helix dipolesNature, 1988