Evidence map›Paper›PMID 31011770›Full record

ArticleCellular and molecular life sciences : CMLS2019

Network mapping of the conformational heterogeneity of SOD1 by deploying statistical cluster analysis of FTIR spectra.

Sourav Chowdhury, Sagnik Sen, Amrita Banerjee, Vladimir N Uversky, Ujjwal Maulik, Krishnananda Chattopadhyay

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In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

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0cells of the map it votes in
4citing papers in PubMed
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1 · What the graph read from it

What it found

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Sourav ChowdhuryProtein Folding and Dynamics Laboratory, Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata, 700032, India.
Sagnik SenDepartment of Computer Science, Jadavpur University, Kolkata, 700 032, India.
Amrita BanerjeeProtein Folding and Dynamics Laboratory, Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata, 700032, India.
Vladimir N UverskyDepartment of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd. MDC07, Tampa, FL, USA.
Ujjwal MaulikChemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA, 02138, USA.
Krishnananda ChattopadhyayProtein Folding and Dynamics Laboratory, Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata, 700032, India. krish@iicb.res.in.ORCID http://orcid.org/0000-0002-1449-8909

Funding

Science and Engineering Research Board EMR/2016/000310
6 · The paper itself

Abstract

A crucial contribution to the heterogeneity of the conformational landscape of a protein comes from the way an intermediate relates to another intermediate state in its journey from the unfolded to folded or misfolded form. Unfortunately, it is extremely hard to decode this relatedness in a quantifiable manner. Here, we developed an application of statistical cluster analyses to explore the conformational heterogeneity of a metalloenzyme, human cytosolic copper-zinc superoxide dismutase (SOD1), using the inputs from infrared spectroscopy. This study provides a quantifiable picture of how conformational information at one particular site (for example, the copper-binding pocket) is related to the information at the second site (for example, the zinc-binding pocket), and how this relatedness is transferred to the global conformational information of the protein. The distance outputs were used to quantitatively generate a network capturing the folding sub-stages of SOD1.

Indexed as

Binding SitesCloning, MolecularCluster AnalysisCopperEscherichia coliGene ExpressionGenetic VectorsHumansModels, MolecularMutagenesis, Site-DirectedProtein AggregatesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein FoldingProtein Interaction Domains and MotifsCopperProtein AggregatesRecombinant ProteinsSOD1 protein, humanSuperoxide Dismutase-1ZincALSCluster dendrogramCorrelation analysisInfrared spectroscopyProtein aggregationProtein foldingSuperoxide dismutase

Identifiers

PMID31011770
PMCPMC11105373

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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.