Evidence map›Paper›PMID 26147762›Full record

ArticlePloS one2015

Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis.

Prakash Chandra Rathi, Karl-Erich Jaeger, Holger Gohlke

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

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  17. Basal Histamine HChemistry (Weinheim an der Bergstrasse, Germany) · 2019
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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.

Prakash Chandra RathiInstitute of Pharmaceutical and Medical Chemistry, Heinrich-Heine-University, Düsseldorf, Germany.
Karl-Erich JaegerInstitute of Molecular Enzyme Technology, Heinrich-Heine-University, Düsseldorf, Germany; Institute of Bio- and Geosciences IBG-1: Biotechnology, Research Centre Jülich, Jülich, Germany.
Holger GohlkeInstitute of Pharmaceutical and Medical Chemistry, Heinrich-Heine-University, Düsseldorf, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding the origin of thermostability is of fundamental importance in protein biochemistry. Opposing views on increased or decreased structural rigidity of the folded state have been put forward in this context. They have been related to differences in the temporal resolution of experiments and computations that probe atomic mobility. Here, we find a significant (p = 0.004) and fair (R2 = 0.46) correlation between the structural rigidity of a well-characterized set of 16 mutants of lipase A from Bacillus subtilis (BsLipA) and their thermodynamic thermostability. We apply the rigidity theory-based Constraint Network Analysis (CNA) approach, analyzing directly and in a time-independent manner the statics of the BsLipA mutants. We carefully validate the CNA results on macroscopic and microscopic experimental observables and probe for their sensitivity with respect to input structures. Furthermore, we introduce a robust, local stability measure for predicting thermodynamic thermostability. Our results complement work that showed for pairs of homologous proteins that raising the structural stability is the most common way to obtain a higher thermostability. Furthermore, they demonstrate that related series of mutants with only a small number of mutations can be successfully analyzed by CNA, which suggests that CNA can be applied prospectively in rational protein design aimed at higher thermodynamic thermostability.

Indexed as

Bacillus subtilisBacterial ProteinsEnzyme StabilityGenetic VariationHot TemperatureLipaseMolecular Dynamics SimulationMutationThermodynamicsBacterial ProteinsLipase

Identifiers

PMID26147762
PMCPMC4493141

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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.