Helix compactness and stability: Electron structure calculations of conformer dependent thermodynamic functions

Jákli, Imre and Csizmadia, G. Imre and Fejér, N. Szilárd and Farkas, Ödön and Viskolcz, Béla and Jensen, Svend J. Knak and Perczel, András (2013) Helix compactness and stability: Electron structure calculations of conformer dependent thermodynamic functions. CHEMICAL PHYSICS LETTERS, 563. pp. 80-87. ISSN 0009-2614

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Abstract

Structure, stability, cooperativity and molecular packing of two major backbone forms: 310-helix and β-strand are investigated. Long models HCO-(Xxx)n-NH2 Xxx = Gly and (l-)Ala, n ⩽ 34, are studied at two levels of theory including the effect of dispersion forces. Structure and folding preferences are established, the length modulated cooperativity and side-chain determined fold compactness is quantified. By monitoring ΔG°β→α rather than the electronic energy, ΔEβ→α, it appears that Ala is a much better helix forming residue than Gly. The achiral Gly forms a more compact 310-helix than any chiral amino acid residue probed here for l-Ala.

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