Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 284

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Model-Free Approach to the Dynamic Interpretation of Residual Dipolar Couplings in Globular Proteins

Meiler, Jens, Prompers, Jeanine J., Peti, Wolfgang, Griesinger, Christian, Brüschweiler, Rafael·2001·Journal of the American Chemical Society
DOI 10.1021/ja010002z
Open this paper in CoChat — free account

Abstract

The effects of internal motions on residual dipolar NMR couplings of proteins partially aligned in a liquid-crystalline environment are analyzed using a 10 ns molecular dynamics (MD) computer simulation of ubiquitin. For a set of alignment tensors with different orientations and rhombicities, MD-averaged dipolar couplings are determined and subsequently interpreted for different scenarios in terms of effective alignment tensors, average orientations of dipolar vectors, and intramolecular reorientational vector distributions. Analytical relationships are derived that reflect similarities and differences between motional scaling of dipolar couplings and scaling of dipolar relaxation data (NMR order parameters). Application of the self-consistent procedure presented here to dipolar coupling measurements of biomolecules aligned in different liquid-crystalline media should allow one to extract in a "model-free" way average orientations of dipolar vectors and specific aspects of their motions.

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 · 10.1021/ja010002z

Cites

24 of 24 references verified0 citation errors · 0 not checkable

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

Cited by

See all 284

Metadata

Authors
Meiler, J., Prompers, J. J., Peti, W., Griesinger, C., & Brüschweiler, R.
Venue
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Published
2001-05-26
Volume
123
Issue
25
Pages
6098-6107
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
DOI
10.1021/ja010002z
OpenAlex
W2144731691
Cited by
284
References
24
FWCI
11.38
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

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.