Evidence map›Paper›PMID 9566312›Full record

ArticleJournal of biomolecular NMR1998

Chemical shift homology in proteins.

B C Potts, W J Chazin

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

B C PottsDepartment of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
W J Chazin

Funding

STRUCTURE AND REDESIGN OF PROTEIN MANGANESE, IRON AND COPPER SITESP01GM048495 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI PIQUE, MICHAEL E. · 1993 to 2001
$2.3M
NIGMS NIH HHS GM PO1 48495PHS HHS R01 40120
6 · The paper itself

Abstract

The degree of chemical shift similarity for homologous proteins has been determined from a chemical shift database of over 50 proteins representing a variety of families and folds, and spanning a wide range of sequence homologies. After sequence alignment, the similarity of the secondary chemical shifts of C alpha protons was examined as a function of amino acid sequence identity for 37 pairs of structurally homologous proteins. A correlation between sequence identity and secondary chemical shift rmsd was observed. Important insights are provided by examining the sequence identity of homologous proteins versus percentage of secondary chemical shifts that fall within 0.1 and 0.3 ppm thresholds. These results begin to establish practical guidelines for the extent of chemical shift similarity to expect among structurally homologous proteins.

Indexed as

AnimalsCalcium-Binding ProteinsDatabases, FactualHumansMagnetic Resonance SpectroscopyProtein ConformationProteinsSequence Homology, Amino AcidCalcium-Binding ProteinsProteins

Identifiers

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.