Journal article
Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
Biopolymers, Vol.31(13), pp.1463-1470
11/1991
DOI: 10.1002/bip.360311304
PMID: 1814498
Abstract
Thermal unfolding curves have been measured for a series of short alanine‐based peptides that contain repeating sequences and varying chain lengths. Standard helix–coil theory successfully fits the observed transition curves, even for these short peptides. The results provide values for σ, the helix nucleation constant, ΔH°, the enthalpy change on helix formation, and for s(0°C), the average helix propagation parameter at 0°C. The enthalpy change agrees with the value determined calorimetrically. The success of helix–coil theory in describing the unfolding transitions of short peptides in water indicates that helical propensities, or s values, can be determined from substitution experiments in short alanine‐based peptides. Copyright © 1991 John Wiley & Sons, Inc.
Details
- Title: Subtitle
- Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
- Creators
- J. Martin Scholtz - Stanford UniversityHong Qian - University of OregonEunice J. York - University of Colorado HospitalJohn M. Stewart - University of Colorado HospitalRobert L. Baldwin - Stanford University
- Resource Type
- Journal article
- Publication Details
- Biopolymers, Vol.31(13), pp.1463-1470
- Publisher
- Wiley Subscription Services, Inc., A Wiley Company
- DOI
- 10.1002/bip.360311304
- PMID
- 1814498
- ISSN
- 0006-3525
- eISSN
- 1097-0282
- Number of pages
- 8
- Language
- English
- Date published
- 11/1991
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293074202771
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