Evidence map›Paper›PMID 21976375›Full record

ArticleProteins2012

PROTS: a fragment based protein thermo-stability potential.

Yunqi Li, Jian Zhang, David Tai, C Russell Middaugh, Yang Zhang, Jianwen Fang

Abstract read
In one paragraph

Article in Proteins, 2012. 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
–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

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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.

  1. Review
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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

6 authors.

Yunqi LiApplied Bioinformatics Laboratory, the University of Kansas, Lawrence, Kansas 66047, USA.
Jian Zhang
David Tai
C Russell Middaugh
Yang Zhang
Jianwen Fang

Funding

I-TASSER based atomic-level protein structure predictionR01GM083107 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2008 to 2019
$3.5M
Atomic-level, large-scale structure prediction of G protein-coupled receptorsR01GM084222 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2009 to 2012
$1.3M
NIGMS NIH HHS R01 GM083107NIGMS NIH HHS R01 GM084222
6 · The paper itself

Abstract

Designing proteins with enhanced thermo-stability has been a main focus of protein engineering because of its theoretical and practical significance. Despite extensive studies in the past years, a general strategy for stabilizing proteins still remains elusive. Thus effective and robust computational algorithms for designing thermo-stable proteins are in critical demand. Here we report PROTS, a sequential and structural four-residue fragment based protein thermo-stability potential. PROTS is derived from a nonredundant representative collection of thousands of thermophilic and mesophilic protein structures and a large set of point mutations with experimentally determined changes of melting temperatures. To the best of our knowledge, PROTS is the first protein stability predictor based on integrated analysis and mining of these two types of data. Besides conventional cross validation and blind testing, we introduce hypothetical reverse mutations as a means of testing the robustness of protein thermo-stability predictors. In all tests, PROTS demonstrates the ability to reliably predict mutation induced thermo-stability changes as well as classify thermophilic and mesophilic proteins. In addition, this white-box predictor allows easy interpretation of the factors that influence mutation induced protein stability changes at the residue level.

Indexed as

Computer SimulationModels, MolecularProtein StabilitySoftwareAlgorithmsAmino Acid SequenceAnimalsBacterial ProteinsChickensFibroblast Growth Factor 1HumansLinear ModelsMuramidaseMutation, MissenseProtein EngineeringProtein Structure, SecondaryBacterial ProteinsFibroblast Growth Factor 1Muramidasesubtilisin inhibitor protein, Streptomyces

Identifiers

PMID21976375
PMCPMC3407552

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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.