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• W2023100445 endingPage "427" @default.
• W2023100445 startingPage "422" @default.
• W2023100445 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." @default.
• W2023100445 created "2016-06-24" @default.
• W2023100445 creator A5072470570 @default.
• W2023100445 creator A5076751721 @default.
• W2023100445 date "1998-07-01" @default.
• W2023100445 modified "2023-10-10" @default.
• W2023100445 title "A Helix Propensity Scale Based on Experimental Studies of Peptides and Proteins" @default.
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• W2023100445 doi "https://doi.org/10.1016/s0006-3495(98)77529-0" @default.
• W2023100445 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1299714" @default.
• W2023100445 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9649402" @default.
• W2023100445 hasPublicationYear "1998" @default.
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