Evidence map›Paper›PMID 16957327›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2007

Packing regularities in biological structures relate to their dynamics.

Robert L Jernigan, Andrzej Kloczkowski

Abstract readComparative Study
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Computational Ways to Enhance Protein Inhibitor Design.Frontiers in molecular biosciences · 2020
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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.

Robert L JerniganDepartment of Biochemistry, Biophysics, and Molecular Biology, Laurence H. Baker Center for Bioinformatics and Biological Statistics, Iowa State University, Ames, IA, USA.
Andrzej Kloczkowski

Funding

Coarse-Grained Models of ProteinsR01GM072014 · NIGMS · IOWA STATE UNIVERSITY · PI JERNIGAN, ROBERT L · 2004 to 2012
$2.3M
Modeling Ribosomal Control, Function and AssemblyR01GM073095 · NIGMS · IOWA STATE UNIVERSITY · PI JERNIGAN, ROBERT L · 2006 to 2009
$1.0M
NIGMS NIH HHS R01 GM072014NIGMS NIH HHS R01GM072014-01NIGMS NIH HHS R01 GM073095
6 · The paper itself

Abstract

The high packing density inside proteins leads to certain geometric regularities and also is one of the most important contributors to the high extent of cooperativity manifested by proteins in their cohesive domain motions. The orientations between neighboring nonbonded residues in proteins substantially follow the similar geometric regularities, regardless of whether the residues are on the surface or buried, a direct result of hydrophobicity forces. These orientations are relatively fixed and correspond closely to small deformations from those of the face-centered cubic lattice, which is the way in which identical spheres pack at the highest density. Packing density also is related to the extent of conservation of residues, and we show this relationship for residue packing densities by averaging over a large sample or residue packings. There are three regimes: (1) over a broad range of packing densities the relationship between sequence entropy and inverse packing density is nearly linear, (2) over a limited range of low packing densities the sequence entropy is nearly constant, and (3) at extremely low packing densities the sequence entropy is highly variable. These packing results provide important justification for the simple elastic network models that have been shown for a large number of proteins to represent protein dynamics so successfully, even when the models are extremely coarse grained. Elastic network models for polymeric chains are simple and could be combined with these protein elastic networks to represent partially denatured parts of proteins. Finally, we show results of applications of the elastic network model to study the functional motions of the ribosome, based on its known structure. These results indicate expected correlations among its components for the step-wise processing steps in protein synthesis, and suggest ways to use these elastic network models to develop more detailed mechanisms, an important possibility because most experiments yield only static structures.

Indexed as

Genetic VariationModels, ChemicalModels, MolecularProtein ConformationAmino Acid SequenceComputational BiologyProteinsRibosomesSequence AlignmentProteins

Identifiers

PMID16957327
PMCPMC2039702

What OpenQuestion holds

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Read underepoch 390

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.