Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 584

The DOI matches its Crossref record.

Infrared spectroscopy of collagen and collagen‐like polypeptides

Doyle, Barbara Brodsky, Bendit, E. G., Blout, Elkan R.·1975·Biopolymers

Abstract

The set of synthetic polytripeptides and polyhexapeptides which can adopt a triple‐helical form constitute a good model system for investigating collagen structure. Here we consider previous and new infrared spectroscopic studies on collagen and present the infrared spectra of a number of polymers with collagen‐like features. The amide A band position for all triple‐helical polypeptides is higher than that observed for most proteins and polypeptides, and this high frequency appears to be related to the degree of supercoiling of the triple helix. It is possible that with increased supercoiling of the three chains the angles between the groups involved in the intramolecular hydrogen bonds become less favorable, or these bonds may become unusually long. The frequency of the amide I band varies considerably for triple‐helical polypeptides with different amino acid sequences, and often minor bands are observed. This finding contrasts with the observations for polypeptides in a pleated sheet or α‐helical form, where the same amide I frequency is observed regardless of the amino acid composition. An explanation for this variation is proposed in terms of the hydrogen bonding properties of imino acids. Significant spectral changes in the amide I region are observed on hydration in the spectra of some triple‐helical polypeptides, but corresponding changes have not been found in the collagens examined.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1002/bip.1975.360140505

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.

A few free checks a day · papers already verified open instantly · results are public

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

No references could be resolved yet.

Research works printed but not linked: 57

  1. 10.1098/rspa.1951.0016 · DOI
  2. 10.1002/pol.1962.1206217424 · doi:10.1002/pol.1962.1206217424
  3. 10.1063/1.1742489 · DOI · Paper page
  4. 10.1063/1.1744547 · DOI
  5. Bamford C. H., 1956, Synthetic Polypeptides, 157
  6. Miyazawa T., 1963, Aspects of Protein Structure, 260
  7. 10.1016/S0022-2836(62)80132-6 · doi:10.1016/s0022-2836(62)80132-6
  8. 10.1063/1.1731990 · doi:10.1063/1.1731990
  9. 10.1063/1.1730999 · DOI · Paper page
  10. Miyazawa T., 1962, Polyamino Acids, Polypeptides and Proteins, 205
  11. 10.1021/ja01464a042 · DOI · Paper page
  12. 10.1016/0032-3861(63)90007-7 · DOI
  13. Garrigou‐Lagrange C., 1970, J. Chim. Phys. Physicochim. Biol., 67, 1936, 10.1051/jcp/1970671936 · doi:10.1051/jcp/1970671936
  14. Johnston N.(1975) Ph. D. thesis University of Michigan.
  15. Richards R. E.&Thompson H. W.(1947)J. Chem. Soc. 1248–1260. · doi:10.1039/jr9470001248
  16. 10.1021/bi00792a011 · doi:10.1021/bi00792a011
  17. 10.1021/ma60037a010 · doi:10.1021/ma60037a010
  18. 10.1002/bip.360101219 · DOI
  19. 10.1002/bip.360101218 · doi:10.1002/bip.360101218
  20. Chirgadze Yu., 1962, Biofizika, 6, 657
  21. 10.1021/ja00716a013 · DOI
  22. 10.1016/0022-2836(72)90523-2 · doi:10.1016/0022-2836(72)90523-2
  23. 10.1021/bi00792a010 · doi:10.1021/bi00792a010
  24. 10.1021/ja00961a033 · DOI
  25. 10.1016/0022-2836(69)90355-6 · DOI
  26. 10.1246/bcsj.41.1273 · DOI
  27. 10.1039/df9500900378 · doi:10.1039/df9500900378
  28. 10.1098/rspa.1951.0065 · DOI
  29. 10.1039/df9582500173 · doi:10.1039/df9582500173
  30. Seeds W., 1953, Nature and Structure of Collagen, 250
  31. 10.1002/bip.360100913 · DOI
  32. Fraser R. D. B., 1973, Conformation in Fibrous Proteins
  33. Bellamy L. J., 1958, The Infrared Spectra of Complex Molecules, 162
  34. Pimentel G. C., 1960, The Hydrogen Bond, 70
  35. 10.1016/0022-2852(60)90076-X · doi:10.1016/0022-2852(60)90076-x
  36. Fraser R. D. B.(1951) Ph.D. Thesis University of London.
  37. Ramachandran G. N., 1967, Treatise on Collagen, 143
  38. 10.1002/bip.1970.360090808 · doi:10.1002/bip.1970.360090808
  39. 10.1021/ja01515a031 · doi:10.1021/ja01515a031
  40. 10.1051/jcp/1970670959 · doi:10.1051/jcp/1970670959
  41. 10.1038/168325a0 · doi:10.1038/168325a0
  42. 10.1039/tf9565200528 · doi:10.1039/tf9565200528
  43. 10.1002/bip.1966.360040307 · DOI
  44. Andreeva N. S., 1961, Biophysics (U.S.S.R.), 6, 85
  45. Andreeva N. S., 1963, Aspects of Protein Structure, 137
  46. Andreeva N. S., 1970, Biophysics (U.S.S.R.), 15, 204
  47. Shibnev V. A., 1966, Biophysics (U.S.S.R.), 11, 1219
  48. 10.1038/221914a0 · doi:10.1038/221914a0
  49. 10.1016/0022-2836(67)90147-7 · doi:10.1016/0022-2836(67)90147-7
  50. 10.1016/0022-2836(69)90356-8 · DOI
  51. 10.1016/0022-2836(69)90353-2 · DOI
  52. 10.1016/0022-2836(69)90354-4 · doi:10.1016/0022-2836(69)90354-4
  53. 10.1016/0022-2836(72)90175-1 · doi:10.1016/0022-2836(72)90175-1
  54. Susi H., 1969, Structure and Stability of Biological Macromolecules, 589
  55. 10.1016/0005-2795(73)90164-5 · DOI · Paper page
  56. 10.1016/0006-291X(73)90961-3 · DOI · Paper page
  57. 10.1016/0006-291X(73)90960-1 · DOI · Paper page

Cited by

See all 584

Metadata

Authors
Doyle, B. B., Bendit, E. G., & Blout, E. R.
Venue
Biopolymers
Publisher
Wiley
Published
1975-05
Volume
14
Issue
5
Pages
937-957
ISSN
  • 0006-3525 (ISSN-L)
  • 1097-0282
OpenAlex
W2119759524
Cited by
584
References
0
FWCI
3.03
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: Infrared spectroscopy of collagen and collagen‐like polypeptides. https://app.cochat.ai/papers/10.1002/bip.1975.360140505
The paper
Doyle, B. B., Bendit, E. G., & Blout, E. R. (1975). Infrared spectroscopy of collagen and collagen‐like polypeptides. Biopolymers. https://doi.org/10.1002/bip.1975.360140505

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.