The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Theoretical CD studies of polypeptide helices: Examination of important electronic and geometric factors
Abstract
An improved model for calculating the CD of polypeptides has been developed. Excited state wavefunctions were derived from CNDO/S (complete neglect of differential overlap, spectroscopic) calculations on N‐methylacetamide. Four discrete peptide‐localized transitions were employed: π 0 π*(NV 1), π+π* (NV 2), n π*, and n′π*. Inclusion of the π+π*transition (λ 0 = 140 nm) significantly improves the accuracy of the calculated CD spectra in the 180‐250‐nm region. Spectra were computed for various helical structures, including right‐handed α‐, α II‐, ω‐, π‐, 3 10‐, and poly(proline)I‐helices, and the left‐handed poly(proline)II‐helix. Sensitivity to changes in the peptide backbone geometry and chain length are examined. Electronic factors such as ground‐state charge distribution, hybridization effects, and basis set deorthogonalization have been investigated. The nonconservative nature of the poly (Pro) I and II CD spectra is reproduced, and the helix band present in earlier exciton calculations on the α‐helix has been diminished.
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Cites
Electronic Population Analysis on LCAO–MO Molecular Wave Functions. I
Mulliken, R. S. (1955) · The Journal of Chemical Physics · doi:10.1063/1.1740588 · Cited by 11,049
A new force field for molecular mechanical simulation of nucleic acids and proteins
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Löwdin, P.-O. (1950) · The Journal of Chemical Physics · doi:10.1063/1.1747632 · Cited by 3,175
Conformation of Polypeptides and Proteins
Ramachandran, G. N., & Sasisekharan, V. (1968) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60402-7 · Cited by 2,938
Slater, J. C. (1930) · Physical Review · doi:10.1103/physrev.36.57 · Cited by 2,892
Determination of the helix and β form of proteins in aqueous solution by circular dichroism
Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,066
Approximate Self-Consistent Molecular Orbital Theory. I. Invariant Procedures
Pople, J. A., Santry, D. P., & Segal, G. A. (1965) · The Journal of Chemical Physics · doi:10.1063/1.1701475 · Cited by 1,721
Optical Rotatory Dispersion of Helical Polymers
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Atomic Coordinates and Structure Factors for Two Helical Configurations of Polypeptide Chains
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Cited by
Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)
Toniolo, C., Crisma, M., Formaggio, F., & Peggion, C. (2001) · Biopolymers · doi:10.1002/1097-0282(2001)60:6<396::aid-bip10184>3.0.co;2-7 · Cited by 674
Single Turn Peptide Alpha Helices with Exceptional Stability in Water
Shepherd, N. E., Hoang, H. N., Abbenante, G., & Fairlie, D. P. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0456003 · Cited by 326
Grabeck, J., Mayer, J., Miltz, A., Casoria, M., Quagliata, M., Meinberger, D., Klatt, A. R., Wielert, I., Maier, B., Papini, A. M., et al. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00078 · Cited by 7
Metadata
- Authors
- Manning, M. C., & Woody, R. W.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1991-04
- Volume
- 31
- Issue
- 5
- Pages
- 569-586
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W1979528014
- Cited by
- 327
- References
- 24
- FWCI
- 2.66
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
