Transmuting α helices and β sheets
- 1 October 1997
- journal article
- Published by Elsevier in Folding and Design
- Vol. 2 (5) , R71-R79
- https://doi.org/10.1016/s1359-0278(97)00036-9
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- An α to β conformational switch in EF-TuStructure, 1996
- Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet proteinNature Structural & Molecular Biology, 1996
- Context-dependent secondary structure formation of a designed protein sequenceNature, 1996
- Conformational switching in designed peptides: the helix/sheet transitionFolding and Design, 1996
- Stability of α-HelicesPublished by Elsevier ,1995
- A Thermodynamic Scale for the .beta.-Sheet Forming Tendencies of the Amino AcidsBiochemistry, 1994
- Measurement of the β-sheet-forming propensities of amino acidsNature, 1994
- Origins of structural diversity within sequentially identical hexapeptidesProtein Science, 1993
- Dominant forces in protein foldingBiochemistry, 1990
- On the use of sequence homologies to predict protein structure: identical pentapeptides can have completely different conformations.Proceedings of the National Academy of Sciences, 1984