Journal of molecular biology, 1991-05, Vol.219 (2), p.135-137
1991
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- Autor(en) / Beteiligte
- Titel
- Straight-chain non-polar amino acids are good helix-formers in water
- Ist Teil von
- Journal of molecular biology, 1991-05, Vol.219 (2), p.135-137
- Ort / Verlag
- Oxford: Elsevier Ltd
- Erscheinungsjahr
- 1991
- Quelle
- Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
- Beschreibungen/Notizen
- For comparison with earlier data on naturally occurring non-polar amino acids (Ala, Leu, Phe, Val, Ile), the comparative helix-forming tendencies have been measured for non-polar amino acid residues that have unbranched side-chains, with an ethyl, propyl or butyl group, and also for methionine. The substitutions are made in a 17-residue alanine-based peptide. The results show that straight-chain non-polar amino acids have high helix-forming tendencies compared to β-branched non-polar amino acids. Restriction of side-chain conformations in the helix, with a corresponding reduction in conformational entropy, is the likely explanation. There is a small increase in helix-forming tendency as the side-chain increases in length from ethyl to butyl, which suggests that a helix-stabilizing hydrophobic interaction is being detected.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0022-2836eISSN: 1089-8638DOI: 10.1016/0022-2836(91)90553-ITitel-ID: cdi_proquest_miscellaneous_80573540
- Format
- –
- Schlagworte
- Alanine - chemistry, Amino Acid Sequence, Amino Acids - chemistry, Aminoacids, peptides. Hormones. Neuropeptides, Analytical, structural and metabolic biochemistry, Biological and medical sciences, Circular Dichroism, Fundamental and applied biological sciences. Psychology, Isoleucine - chemistry, Leucine - chemistry, Molecular Sequence Data, non-polar side-chains, Peptides - chemistry, Phenylalanine - chemistry, Protein Conformation, Proteins, Valine - chemistry, Water, α-helix propensity