The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
The Stereochemistry of Peptides Containing α-Aminoisobutyric Aci
Abstract
The introduction of alpha-aminoisobutyric acid (Aib) into peptides dramatically limits the range of accessible backbone conformations. The presence of two geminal methyl groups at C alpha sterically compels Aib residues to largely favor structures in the right- or left-handed 3(10)/alpha-helical regions (phi approximately +/- 60 +/- 20 degrees, psi approximately +/- 30 +/- 20 degrees) of the peptide conformational map. Aib residues occur extensively in microbial peptides which form transmembrane channels. This observation has stimulated considerable interest in the stereochemistry of Aib peptides. This review summarizes theoretical studies on the conformations of Aib residues and examines the available data on solid-state structures, derived from single crystal X-ray diffraction studies. Crystal structures of over three dozen Aib-containing peptides, ranging in length from 2 to 11 residues, have been reported so far which exemplify various types of beta-turns, consecutive beta-turns, and helical structures. Examples of nonhydrogen bonded and cyclic structures are also described. The crystallographic results compare well with structural studies in solution, establishing that Aib peptides can provide rigid structural models for the development of spectroscopic methods of peptide conformational analysis.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Stereochemistry of polypeptide chain configurations
Ramachandran, G. N., Ramakrishnan, C., & Sasisekharan, V. (1963) · Journal of Molecular Biology · doi:10.1016/s0022-2836(63)80023-6 · Cited by 3,554
Empirical Predictions of Protein Conformation
Chou, P. Y., & Fasman, G. D. (1978) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.47.070178.001343 · Cited by 3,124
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
Venkatachalam, C. M. (1968) · Biopolymers · doi:10.1002/bip.1968.360061006 · Cited by 1,511
Chou, P. Y., & Fasman, G. D. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90094-8 · Cited by 956
Fox, R. O., & Richards, F. M. (1982) · Nature · doi:10.1038/300325a0 · Cited by 718
The Gramicidin A Transmembrane Channel: A Proposed π (L,D) Helix
Urry, D. W. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.3.672 · Cited by 667
Lewis, P. N., Momany, F. A., & Scheraga, H. A. (1973) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(73)90350-4 · Cited by 659
Action Potentials induced in Biomolecular Lipid Membranes
MUELLER, P., & RUDIN, D. O. (1968) · Nature · doi:10.1038/217713a0 · Cited by 504
Reverse Turns in Peptides and Protein
Smith, J. A., Pease, L. G., & Kopple, K. D. (1980) · Critical Reviews in Biochemistry · doi:10.3109/10409238009105470 · Cited by 501
Cited by
Structural characteristics of .alpha.-helical peptide molecules containing Aib residues
Karle, I. L., & Balaram, P. (1990) · Biochemistry · doi:10.1021/bi00481a001 · Cited by 989
Self-citationVasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P. (2011) · Chemical Reviews · doi:10.1021/cr100100x · Cited by 329
Self-citationVass, E., Hollósi, M., Besson, F., & Buchet, R. (2003) · Chemical Reviews · doi:10.1021/cr000100n · Cited by 288
Structures of peptides from α‐amino acids methylated at the α‐carbon,
Toniolo, C., Crisma, M., Formaggio, F., Valle, C., Cavicchioni, G., Precigoux, G., Aubry, A., & Kamphuis, J. (1993) · Biopolymers · doi:10.1002/bip.360330708 · Cited by 238
Karle, I. L., Flippen-Anderson, J. L., Uma, K., Balaram, H., & Balaram, P. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.3.765 · Cited by 70
Self-citation
Metadata
- Authors
- Venkataram Prasad, B. V., Balaram, P., & Benedetti, E.
- Venue
- Critical Reviews in Biochemistry
- Publisher
- Informa UK Limited
- Published
- 1984-01
- Volume
- 16
- Issue
- 4
- Pages
- 307-348
- ISSN
- 0045-6411 (ISSN-L)
- 1040-8355
- OpenAlex
- W2206170546
- Cited by
- 339
- References
- 37
- FWCI
- 2.28
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The Stereochemistry of Peptides Containing α-Aminoisobutyric Aci. https://app.cochat.ai/papers/10.3109/10409238409108718
- The paper
- Venkataram Prasad, B. V., Balaram, P., & Benedetti, E. (1984). The Stereochemistry of Peptides Containing α-Aminoisobutyric Aci. Critical Reviews in Biochemistry. https://doi.org/10.3109/10409238409108718
Data sources
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.