On the band gap in peptide alpha-helices

Herz T, Otto P, Clark T (2000)


Publication Status: Published

Publication Type: Journal article

Publication year: 2000

Journal

Publisher: Wiley-Blackwell

Book Volume: 79

Pages Range: 120-124

Journal Issue: 2

DOI: 10.1002/1097-461X(2000)79:2<120::AID-QUA7>3.0.CO;2-1

Abstract

The variation in the band gap of a (Gly)(30) alpha-helix with position in the peptide sequence has been investigated using AM1 semiempirical molecular orbital (MO) theory within an extensive singles configuration interaction (CI) treatment. The dipole-charge interaction along the length of the helix results in the highest local electron affinity near the N-terminus and the lowest local ionization potential near the C-terminus. The calculations suggest that the band gap, measured as the difference between the local ionization potential and electron affinity decreases from the C-terminus to the N-terminus for the model (Gly)(30) alpha-helix in vacuo. (C) 2000 John Wiley & Sons, Inc.

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How to cite

APA:

Herz, T., Otto, P., & Clark, T. (2000). On the band gap in peptide alpha-helices. International Journal of Quantum Chemistry, 79(2), 120-124. https://dx.doi.org/10.1002/1097-461X(2000)79:2<120::AID-QUA7>3.0.CO;2-1

MLA:

Herz, Thomas, Peter Otto, and Timothy Clark. "On the band gap in peptide alpha-helices." International Journal of Quantum Chemistry 79.2 (2000): 120-124.

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