The relationship between sequence and structure in elementary folding units
- 1 January 2000
- book chapter
- Published by Elsevier in Advances in Protein Chemistry
- Vol. 53, 49-85
- https://doi.org/10.1016/s0065-3233(00)53002-2
Abstract
No abstract availableKeywords
This publication has 147 references indexed in Scilit:
- Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequenceJournal of Molecular Biology, 1997
- Folding kinetics of Che Y mutants with enhanced native α-helix propensities 1 1Edited by A. R. FershtJournal of Molecular Biology, 1997
- Contribution of the Hydrophobic Effect to the Stability of Human Lysozyme: Calorimetric Studies and X-ray Structural Analyses of the Nine Valine to Alanine Mutants,Biochemistry, 1997
- Helix propagation and N‐cap propensities of the amino acids measured in alanine‐based peptides in 40 volume percent trifluoroethanolProtein Science, 1996
- Comparison between the φ Distribution of the Amino Acids in the Protein Database and NMR Data Indicates that Amino Acids have Various φ Propensities in the Random Coil ConformationJournal of Molecular Biology, 1995
- Experimental Analysis of the Schellman MotifJournal of Molecular Biology, 1995
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- Local Conformations of Peptides Representing the Entire Sequence of Bovine Pancreatic Trypsin Inhibitor and Their Roles in FoldingJournal of Molecular Biology, 1993
- Solvation energy in protein folding and bindingNature, 1986
- Conformation of twisted β-pleated sheets in proteinsJournal of Molecular Biology, 1973