CD Spectroscopy and the Helix-Coil Transition in Peptides and Polypeptides
- 1 January 1996
- book chapter
- Published by Springer Nature
Abstract
No abstract availableKeywords
This publication has 99 references indexed in Scilit:
- Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactionsProtein Science, 1994
- Determination of α-Helix Propensity within the Context of a Folded ProteinJournal of Molecular Biology, 1994
- Contribution of Buried Hydrogen Bonds to Protein Stability The Crystal Structures of Two Barnase MutantsJournal of Molecular Biology, 1993
- Energetic contribution of solvent-exposed ion pairs to alpha-helix structureJournal of Molecular Biology, 1992
- Straight-chain non-polar amino acids are good helix-formers in waterJournal of Molecular Biology, 1991
- Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroismJournal of Molecular Biology, 1980
- Conformational studies on copolymers of L‐leusine and L‐leucine: Circular dichroism and potentiometric titration studiesBiopolymers, 1972
- Conformational studies on copolymers of hydroxypropyl-L-glutamine and L-leucine. Circular dichroism studiesBiochemistry, 1972
- Thermodynamic parameters of helix‐coil transition in polypeptide chains I. Poly‐(L‐glutamic acid)Biopolymers, 1971
- Conformation changes in the nonionizable water‐soluble synthetic polypeptide poly‐N5‐(3‐hydroxypropyl) ‐L‐glutamineBiopolymers, 1965