Solvent Effects on the 310-/α-Helix Equilibrium in Short Amphipathic Peptides Rich in α,α-Disubstituted Amino Acids
- 1 February 1997
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 119 (5), 1167-1168
- https://doi.org/10.1021/ja962875c
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- De Novo Antimicrobial Peptides with Low Mammalian Cell ToxicityJournal of Medicinal Chemistry, 1996
- Antimicrobial α,α-Dialkylated Amino Acid Rich Peptides with in-Vivo Activity against an Intracellular PathogenJournal of Medicinal Chemistry, 1996
- Helical Stability of de Novo Designed .alpha.-Aminoisobutyric Acid-Rich Peptides at High TemperaturesBiochemistry, 1995
- Evidence for a 310‐helical conformation of an eight‐residue peptide from 1H‐ 1H rotating frame overhauser studiesBiopolymers, 1993
- DOMAIN CLOSURE IN MITOCHONDRIAL ASPARTATE-AMINOTRANSFERASEJournal of Molecular Biology, 1992
- Expounding endocrinologyTrends in Biochemical Sciences, 1991
- Conformational preferences of oligopeptides rich in α‐aminoisobutyric acid. I. Observation of a 310/α‐helical transition upon sequence permutationBiopolymers, 1991
- Analysis of protein loop closure: Two types of hinges produce one motion in lactate dehydrogenaseJournal of Molecular Biology, 1991
- Helix geometry in proteinsJournal of Molecular Biology, 1988
- Circular dichroism studies of helical oligopeptides: Can 310 and α‐helical conformations be chiroptically distinguished?International Journal of Peptide and Protein Research, 1983