Conformational switching in designed peptides: the helix/sheet transition
- 1 April 1996
- journal article
- Published by Elsevier in Folding and Design
- Vol. 1 (2) , 91-101
- https://doi.org/10.1016/s1359-0278(96)00018-1
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Prion Protein Peptides Induce .alpha.-Helix to .beta.-Sheet Conformational TransitionsBiochemistry, 1995
- Importance of Environment in Determining Secondary Structure in ProteinsBiochemistry, 1994
- Origins of structural diversity within sequentially identical hexapeptidesProtein Science, 1993
- Redox control of secondary structure in a designed peptideJournal of the American Chemical Society, 1993
- NMR studies of amyloid .beta.-peptides: proton assignments, secondary structure, and mechanism of an .alpha.-helix .fwdarw. .beta.-sheet conversion for a homologous, 28-residue, N-terminal fragmentBiochemistry, 1992
- Environment affects amino acid preference for secondary structure.Proceedings of the National Academy of Sciences, 1992
- Switch Peptides: pH‐Induced α‐Helix to β‐Sheet Transitions of Bis‐amphiphilic OligopeptidesAngewandte Chemie International Edition in English, 1991
- Peptides as Conformational Switch: Medium‐Induced Conformational Transitions of Designed PeptidesAngewandte Chemie International Edition in English, 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
- THE FAR ULTRAVIOLET ABSORPTION SPECTRA OF POLYPEPTIDE AND PROTEIN SOLUTIONS AND THEIR DEPENDENCE ON CONFORMATIONProceedings of the National Academy of Sciences, 1961