Evidence map›Paper›PMID 20083491›Full record

ArticleProtein engineering, design & selection : PEDS2010

Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold.

Eric D Merkley, William W Parson, Valerie Daggett

Open access · bronzeAbstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 39 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Eric D MerkleyDepartment of Biochemistry, University of Washington, Box 357350, Seattle, Washington 98195-7350, USA.
William W Parson
Valerie Daggett
University of Washington · US

Funding

MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR01GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 2000 to 2014
$3.9M
MULTI-TIERED PROTEOMIC COMPUTE CLUSTER: PARKINSON'S DISEASES10RR023044 · NCRR · UNIVERSITY OF WASHINGTON · PI GOODLETT, DAVID ROBINSON · 2006 to 2006
$500k
MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR29GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 1995 to 1999
–
NCRR NIH HHS 1S10RR023044-01NIGMS NIH HHS GM 50789PHS HHS TG 32008268
6 · The paper itself

Abstract

A widely held hypothesis regarding the thermostability of thermophilic proteins states asserts that, at any given temperature, thermophilic proteins are more rigid than their mesophilic counterparts. Many experimental and computational studies have addressed this question with conflicting results. Here, we compare two homologous enzymes, one mesophilic (Escherichia coli FMN-dependent nitroreductase; NTR) and one thermophilic (Thermus thermophilus NADH oxidase; NOX), by multiple molecular dynamics simulations at temperatures from 5 to 100 degrees C. We find that the global rigidity/flexibility of the two proteins, assessed by a variety of metrics, is similar on the time scale of our simulations. However, the thermophilic enzyme retains its native conformation to a much greater degree at high temperature than does the mesophilic enzyme, both globally and within the active site. The simulations identify the helix F-helix G 'arm' as the region with the greatest difference in loss of native contacts between the two proteins with increasing temperature. In particular, a network of electrostatic interactions holds helix F to the body of the protein in the thermophilic protein, and this network is absent in the mesophilic counterpart.

Indexed as

Models, MolecularProtein ConformationTemperatureAmino Acid SequenceEscherichia coli ProteinsFMN ReductaseMolecular Dynamics SimulationMolecular Sequence DataMultienzyme ComplexesNADH, NADPH OxidoreductasesNitroreductasesSequence AlignmentThermus thermophilusEscherichia coli ProteinsFMN ReductaseMultienzyme ComplexesNADH, NADPH OxidoreductasesNADH oxidaseNitroreductases

Identifiers

PMID20083491
PMCPMC2851445
OpenAlexW2136718417

What OpenQuestion holds

Textmetadata
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.