Highly restricted distributions of hydrophobic and charged amino acids in longitudinal quadrants of alpha-helices
Department of Pharmacology; Program in Molecular Medicine
*Amino Acids; *Protein Conformation
Life Sciences | Medicine and Health Sciences
Helix formation in folding proteins is stabilized by binding of recurrent hydrophobic side chains in one longitudinal quadrant against the locally most hydrophobic region of the protein. To test this hypothesis, we fitted sequences of 247 alpha-helices of 55 proteins to the circular (infinite) template (symbol; see text) to maximize the strip-of-helix hydrophobicity index (the mean hydrophobicity of residues in (symbol; see text) positions). These template-predicted configurations closely matched crystallographic structures in 87% of four- or five-turn helices compared. We determined the longitudinal quadrant distributions of amino acids in the template-fitted, sheet projections of alpha-helices with respect to the best longitudinal, hydrophobic strip on each helix and to the N and C termini, interiors, and entire helices. Amino acids Leu, Ile, Val, and Phe were concentrated in one longitudinal quadrant (p less than 0.001). Lys, Arg, Asp, and Glu were not in the quadrant of Leu, Ile, Val, and Phe (p less than 0.001). Significant quadrant distributions for other amino acids and for termini of the helices were also found.
J Biol Chem. 1991 Mar 25;266(9):5521-4.
The Journal of biological chemistry
Torgerson RR, Lew RA, Reyes VE, Hardy LW, Humphreys RE. (1991). Highly restricted distributions of hydrophobic and charged amino acids in longitudinal quadrants of alpha-helices. Open Access Articles. Retrieved from https://escholarship.umassmed.edu/oapubs/854