The DOI matches its Crossref record.
Infrared Spectra and Protein Conformations in Aqueous Solutions
Open accessAbstract
Infrared spectra in the region of the amide I' band have been determined for a number of proteins in D2O solution. Comparison of the observed band positions with structural analyses based on optical rotatory dispersion and circular dichroism data, as well as with crystallographically determined structures, indicates that this technique may be useful in conformational studies of proteins in solution.
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
Cited by
Infrared spectroscopy of proteins
Barth, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.004 · Cited by 5,129
“Probably the most common application of infrared spectroscopy in protein studies is the analysis of secondary structure [1,3,4,6,8 – 10, 221, 222 ].”
BackgroundExamination of the secondary structure of proteins by deconvolved FTIR spectra
Byler, D. M., & Susi, H. (1986) · Biopolymers · doi:10.1002/bip.360250307 · Cited by 3,003
Self-citationFTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Infrared Spectroscopic Studies of Lyophilization‐ and Temperature‐Induced Protein Aggregation
Dong, A., Prestrelski, S. J., Dean Allison, S., & Carpenter, J. F. (1995) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.2600840407 · Cited by 458
INFRARED AND LASER‐RAMAN SPECTROSCOPIC STUDIES OF THERMALLY‐INDUCED GLOBULAR PROTEIN GELS
CLARK, A. H., SAUNDERSON, D. H. P., & SUGGETT, A. (1981) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1981.tb02002.x · Cited by 286
Metadata
- Authors
- Timasheff, S. N., Susi, H., & Stevens, L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1967-12
- Volume
- 242
- Issue
- 23
- Pages
- 5467-5473
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1567873486
- Cited by
- 183
- References
- 0
- FWCI
- 3.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
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 Spectra and Protein Conformations in Aqueous Solutions. https://app.cochat.ai/papers/10.1016/s0021-9258(18)99382-8
- The paper
- Timasheff, S. N., Susi, H., & Stevens, L. (1967). Infrared Spectra and Protein Conformations in Aqueous Solutions. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)99382-8
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.