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• W2124767416 endingPage "754" @default.
• W2124767416 startingPage "750" @default.
• W2124767416 abstract "Surveys of protein crystal structures have revealed that amino acids show unique structural preferences for the N1, N2, and N3 positions in the first turn of the α-helix. We have therefore extended helix-coil theory to include statistical weights for these locations. The helix content of a peptide in this model is a function of N-cap, C-cap, N1, N2, N3, C1, and helix interior (N4 to C2) preferences. The partition function for the system is calculated using a matrix incorporating the weights of the fourth residue in a hexamer of amino acids and is implemented using a FORTRAN program. We have applied the model to calculate the N1 preferences of Gln, Val, Ile, Ala, Met, Pro, Leu, Thr, Gly, Ser, and Asn, using our previous data on helix contents of peptides Ac-XAKAAAAKAAGY-CONH2. We find that Ala has the highest preference for the N1 position. Asn is the most unfavorable, destabilizing a helix at N1 by at least 1.4 kcal mol−1 compared to Ala. The remaining amino acids all have similar preferences, 0.5 kcal mol−1 less than Ala. Gln, Asn, and Ser, therefore, do not stabilize the helix when at N1." @default.
• W2124767416 created "2016-06-24" @default.
• W2124767416 creator A5005165880 @default.
• W2124767416 creator A5024338298 @default.
• W2124767416 creator A5024433036 @default.
• W2124767416 date "2008-12-31" @default.
• W2124767416 modified "2023-09-27" @default.
• W2124767416 title "Determination of α-helix N1 energies after addition of N1, N2, and N3 preferences to helix/coil theory" @default.
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• W2124767416 doi "https://doi.org/10.1110/ps.9.4.750" @default.
• W2124767416 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2144615" @default.
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