The DOI matches its Crossref record.
The function of tryptophan residues in membrane proteins
Abstract
Membrane proteins have a significantly higher Trp content than do soluble proteins. This is especially true for the M and L subunits of the photosynthetic reaction center from purple bacteria. The Trp residues are not uniformly distributed through the membrane but are concentrated at the periplasmic side of the complex. In addition, Trp residues are not randomly aligned. Within the protein subunits, many form hydrogen bonds with carbonyl oxygens of the main chain, thereby stabilizing the protein. On the surface of the molecule, they are correctly positioned to form hydrogen bonds with the lipid head groups while their hydrophobic rings are immersed in the lipid part of the bilayer. These observations suggest that Trp residues are involved in the translocation of protein through the membrane and that following translocation, Trp residues serve as anchors on the periplasmic side of the membrane.
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
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
White, S. H., & Wimley, W. C. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.319 · Cited by 1,764
Hydrophobic mismatch between proteins and lipids in membranes
Killian, J. A. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(98)00017-3 · Cited by 632
Vogel, H. J., Schibli, D. J., Jing, W., Lohmeier-Vogel, E. M., Epand, R. F., & Epand, R. M. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-213 · Cited by 353
Multipass membrane protein structure prediction using Rosetta
Yarov‐Yarovoy, V., Schonbrun, J., & Baker, D. (2006) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20817 · Cited by 323
Chikindas, M. L., García-Garcerá, M. J., Driessen, A. J., Ledeboer, A. M., Nissen-Meyer, J., Nes, I. F., Abee, T., Konings, W. N., & Venema, G. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.11.3577-3584.1993 · Cited by 266
Metadata
- Authors
- Schiffer, M., Chang, C.-H., & Stevens, F. J.
- Venue
- "Protein Engineering, Design and Selection"
- Publisher
- Oxford University Press (OUP)
- Published
- 1992
- Volume
- 5
- Issue
- 3
- Pages
- 213-214
- ISSN
- 0269-2139 (ISSN-L)
- 1741-0126
- 1741-0134
- OpenAlex
- W2080044891
- Cited by
- 346
- References
- 0
- FWCI
- 3.44
- 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 function of tryptophan residues in membrane proteins. https://app.cochat.ai/papers/10.1093/protein/5.3.213
- The paper
- Schiffer, M., Chang, C.-H., & Stevens, F. J. (1992). The function of tryptophan residues in membrane proteins. "Protein Engineering, Design and Selection". https://doi.org/10.1093/protein/5.3.213
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.
