Evidence map›Paper›PMID 25330965›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2015

The use of experimental structures to model protein dynamics.

Ataur R Katebi, Kannan Sankar, Kejue Jia, Robert L Jernigan

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Functional Protein Dynamics Directly from Sequences.The journal of physical chemistry. B · 2023
    Article
  3. Article
  4. Article
  5. 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

4 authors at 1 institution in 1 country.

Ataur R KatebiNational Cancer Institute, National Institute of Health, 37 Convent Drive Bldg 37, Bethesda, MD, 20892, USA.
Kannan Sankar
Kejue Jia
Robert L Jernigan
National Cancer Institute · US

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 R01GM072014NIGMS NIH HHS R01 GM073095
6 · The paper itself

Abstract

The number of solved protein structures submitted in the Protein Data Bank (PDB) has increased dramatically in recent years. For some specific proteins, this number is very high-for example, there are over 550 solved structures for HIV-1 protease, one protein that is essential for the life cycle of human immunodeficiency virus (HIV) which causes acquired immunodeficiency syndrome (AIDS) in humans. The large number of structures for the same protein and its variants include a sample of different conformational states of the protein. A rich set of structures solved experimentally for the same protein has information buried within the dataset that can explain the functional dynamics and structural mechanism of the protein. To extract the dynamics information and functional mechanism from the experimental structures, this chapter focuses on two methods-Principal Component Analysis (PCA) and Elastic Network Models (ENM). PCA is a widely used statistical dimensionality reduction technique to classify and visualize high-dimensional data. On the other hand, ENMs are well-established simple biophysical method for modeling the functionally important global motions of proteins. This chapter covers the basics of these two. Moreover, an improved ENM version that utilizes the variations found within a given set of structures for a protein is described. As a practical example, we have extracted the functional dynamics and mechanism of HIV-1 protease dimeric structure by using a set of 329 PDB structures of this protein. We have described, step by step, how to select a set of protein structures, how to extract the needed information from the PDB files for PCA, how to extract the dynamics information using PCA, how to calculate ENM modes, how to measure the congruency between the dynamics computed from the principal components (PCs) and the ENM modes, and how to compute entropies using the PCs. We provide the computer programs or references to software tools to accomplish each step and show how to use these programs and tools. We also include computer programs to generate movies based on PCs and ENM modes and describe how to visualize them.

Indexed as

Models, MolecularDatabases, ProteinEntropyHIV ProteaseHumansPrincipal Component AnalysisHIV Proteasep16 protease, Human immunodeficiency virus 1

Identifiers

PMID25330965
PMCPMC4206088
OpenAlexW2409337192

What OpenQuestion holds

Textmetadata
LicenceTDM
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.