Journal article
Helix Propensities Are Identical in Proteins and Peptides
Biochemistry (Easton), Vol.36(36), pp.10923-10929
09/09/1997
DOI: 10.1021/bi9707180
PMID: 9283083
Abstract
Our understanding of the factors stabilizing α-helical structure has been greatly enhanced by the study of model α-helical peptides. However, the relationship of these results to the folding of helices in intact proteins is not well characterized. Helix propensities measured in model peptides are not in good agreement with those from proteins. In order to address these questions, we have measured helix propensities in the α-helix of ribonuclease T1 and a helical peptide of identical sequence. We have previously demonstrated excellent agreement between peptide and protein for the nonpolar amino acids [Myers, J. K., Pace, C. N., and Scholtz, J. M. (1997) Proc. Natl. Acad. Sci. U.S.A.94, 2833−2837]. Most other amino acids also show good agreement, although certain polar amino acids are exceptions. Helix propensities measured in the ribonuclease T1 peptide/protein are compared with those measured in other systems. Reasonable agreement is found between most systems; however, our propensities differ substantially from those measured in several model peptide systems. Alanine-based peptides overestimate the propensity differences by a factor of 2, and host/guest experiments underestimate them by a factor of 2−3.
Details
- Title: Subtitle
- Helix Propensities Are Identical in Proteins and Peptides
- Creators
- Jeffrey K. Myers - Texas A&M UniversityC. Nick Pace - Department of Medical Biochemistry and Genetics, Department of Biochemistry and Biophysics, and Center forMacromolecular Design, Texas A&M University, College Station, Texas 77843J. Martin Scholtz - Texas A&M University
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.36(36), pp.10923-10929
- Publisher
- American Chemical Society
- DOI
- 10.1021/bi9707180
- PMID
- 9283083
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 09/09/1997
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293076802771
Metrics
67 Record Views