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-helix for all 20 amino acids
Department of Biomolecular Sciences, UMIST, Manchester M60 1QD, UK
Reprint requests to: Dr. Andrew J. Doig, Department of Biomolecular Sciences, UMIST, Manchester M60 1QD, UK; e-mail: Andrew.Doig{at}umist.ac.uk; fax: 44-161-236-0409.
N1 is the first residue in an 
-helix. We have measured the contribution of all 20 amino acids to the stability of a small helical peptide CH3CO-XAAAAQAAAAQAAGY-NH2 at the N1 position. By substituting every residue into the N1 position, we were able to investigate the stabilizing role of each amino acid in an isolated context. The helix content of each of the 20 peptides was measured by circular dichroism (CD) spectroscopy. The data were analyzed by our modified Lifson-Roig helix-coil theory, which includes the n1 parameter, to find free energies for placing a residue into the N1 position. The rank order for free energies is Asp-, Ala > Glu- > Glu0 > Trp, Leu, Ser > Asp0, Thr, Gln, Met, Ile > Val, Pro > Lys+, Arg, His0 > Cys, Gly > Phe > Asn, Tyr, His+. N1 preferences are clearly distinct from preferences for the preceding N-cap and -helix interior. pKa values were measured for Asp, Glu, and His, and protonation-free energies were calculated for Asp and Glu. The dissociation of the Asp proton is less favorable than that of Glu, and this reflects its involvement in a stronger stabilizing interaction at the N terminus. Proline is not energetically favored at the -helix N terminus despite having a high propensity for this position in crystal structures. The data presented are of value both in rationalizing mutations at N1 -helix sites in proteins and in predicting the helix contents of peptides.
Keywords: -Helix; N1 position; circular dichroism; protein folding; protein stability; helix propensities; helix-coil theory; macrodipole
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