Journal article
A helix propensity scale based on experimental studies of peptides and proteins
Biophysical journal, Vol.75(1), pp.422-427
07/01/1998
DOI: 10.1016/S0006-3495(98)77529-0
PMCID: PMC1299714
PMID: 9649402
Abstract
The average globular protein contains 30% alpha-helix, the most common type of secondary structure. Some amino acids occur more frequently in alpha-helices than others; this tendency is known as helix propensity. Here we derive a helix propensity scale for solvent-exposed residues in the middle positions of alpha-helices. The scale is based on measurements of helix propensity in 11 systems, including both proteins and peptides. Alanine has the highest helix propensity, and, excluding proline, glycine has the lowest, approximately 1 kcal/mol less favorable than alanine. Based on our analysis, the helix propensities of the amino acids are as follows (kcal/mol): Ala = 0, Leu = 0.21, Arg = 0.21, Met = 0.24, Lys = 0.26, Gln = 0.39, Glu = 0.40, Ile = 0.41, Trp = 0.49, Ser = 0.50, Tyr = 0. 53, Phe = 0.54, Val = 0.61, His = 0.61, Asn = 0.65, Thr = 0.66, Cys = 0.68, Asp = 0.69, and Gly = 1.
Details
- Title: Subtitle
- A helix propensity scale based on experimental studies of peptides and proteins
- Creators
- C N Pace - Texas A&M UniversityJ M Scholtz - Texas A&M University
- Resource Type
- Journal article
- Publication Details
- Biophysical journal, Vol.75(1), pp.422-427
- DOI
- 10.1016/S0006-3495(98)77529-0
- PMID
- 9649402
- PMCID
- PMC1299714
- NLM abbreviation
- Biophys J
- ISSN
- 0006-3495
- eISSN
- 1542-0086
- Language
- English
- Date published
- 07/01/1998
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293077902771
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