CalFitter 2.0: Leveraging the power of singular value decomposition to analyse protein thermostability

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F22%3A00077619" target="_blank" >RIV/00159816:_____/22:00077619 - isvavai.cz</a>

Alternative codes found

RIV/00216305:26230/22:PU147244 RIV/00216224:14310/22:00126370

Result on the web

<a href="https://academic.oup.com/nar/article/50/W1/W145/6586862?login=true" target="_blank" >https://academic.oup.com/nar/article/50/W1/W145/6586862?login=true</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/nar/gkac378" target="_blank" >10.1093/nar/gkac378</a>

Result language

angličtina

Original language name

CalFitter 2.0: Leveraging the power of singular value decomposition to analyse protein thermostability

Original language description

The importance of the quantitative description of protein unfolding and aggregation for the rational design of stability or understanding the molecular basis of protein misfolding diseases is well established. Protein thermostability is typically assessed by calorimetric or spectroscopic techniques that monitor different complementary signals during unfolding. The CalFitter webserver has already proved integral to deriving invaluable energy parameters by global data analysis. Here, we introduce CalFitter 2.0, which newly incorporates singular value decomposition (SVD) of multi-wavelength spectral datasets into the global fitting pipeline. Processed time- or temperature-evolved SVD components can now be fitted together with other experimental data types. Moreover, deconvoluted basis spectra provide spectral fingerprints of relevant macrostates populated during unfolding, which greatly enriches the information gains of the CalFitter output. The SVD analysis is fully automated in a highly interactive module, providing access to the results to users without any prior knowledge of the underlying mathematics. Additionally, a novel data uploading wizard has been implemented to facilitate rapid and easy uploading of multiple datasets. Together, the newly introduced changes significantly improve the user experience, making this software a unique, robust, and interactive platform for the analysis of protein thermal denaturation data. The webserver is freely accessible at https://loschmidt.chemi.muni.cz/calfitter. [GRAPHICS] .

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2022

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Nucleic Acids Research

ISSN

0305-1048

e-ISSN

1362-4962

Volume of the periodical

50

Issue of the periodical within the volume

W1

Country of publishing house

GB - UNITED KINGDOM

Number of pages

7

Pages from-to

"W145"-"W151"

UT code for WoS article

000796682400001

EID of the result in the Scopus database

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