Evidence map›Paper›PMID 10535950›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Measures of residue density in protein structures.

F Baud, S Karlin

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016
    Review
  9. Article
  10. The role of flexibility and molecular shape in the crystallization of proteins by surface mutagenesis.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Folding without charges.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. Structure of the putative dihydroorotate dehydrogenase from Streptococcus mutans.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    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.

F BaudDepartment of Mathematics, Stanford University, Stanford, CA 94305-2125, USA.
S Karlin

Funding

THEORY &APPLIED STUDIES IN EVOLUTIONARY GENETICSR01GM010452 · NIGMS · STANFORD UNIVERSITY · PI KARLIN, SAMUEL · 1985 to 2006
$2.1M
MOLECULAR SEQUENCE DATAR01HG000335 · NHGRI · STANFORD UNIVERSITY · PI KARLIN, SAMUEL · 1990 to 2001
$449k
NHGRI NIH HHS 5RO1HG00335-11NIGMS NIH HHS 5RO1GM10452-34NIGMS NIH HHS R01 GM010452
6 · The paper itself

Abstract

A hierarchy of residue density assessments and packing properties in protein structures are contrasted, including a regular density, a variety of charge densities, a hydrophobic density, a polar density, and an aromatic density. These densities are investigated by alternative distance measures and also at the interface of multiunit structures. Amino acids are divided into nine structural categories according to three secondary structure states and three solvent accessibility levels. To take account of amino acid abundance differences across protein structures, we normalize the observed density by the expected density defining a density index. Solvent accessibility levels exert the predominant influence in determinations of the regular residue density. Explicitly, the regular density values vary approximately linearly with respect to solvent accessibility levels, the linearity parameters depending on the amino acid. The charge index reveals pronounced inequalities between lysine and arginine in their interactions with acidic residues. The aromatic density calculations in all structural categories parallel the regular density calculations, indicating that the aromatic residues are distributed as a random sample of all residues. Moreover, aromatic residues are found to be over-represented in the neighborhood of all amino acids. This result might be attributed to nucleation sites and protein stability being substantially associated with aromatic residues.

Indexed as

Protein ConformationAmino AcidsAmino Acids

Identifiers

PMID10535950
PMCPMC22960

What OpenQuestion holds

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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.