Protein flexibility in the light of structural alphabets. n

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F15%3A00457876" target="_blank" >RIV/86652036:_____/15:00457876 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.3389/fmolb.2015.00020" target="_blank" >http://dx.doi.org/10.3389/fmolb.2015.00020</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3389/fmolb.2015.00020" target="_blank" >10.3389/fmolb.2015.00020</a>

Result language

angličtina

Original language name

Protein flexibility in the light of structural alphabets. n

Original language description

Protein structures are valuable tools to understand protein function. Nonetheless, proteins are often considered as rigid macromolecules while their structures exhibit specific flexibility, which is essential to complete their functions. Analyses of protein structures and dynamics are often performed with a simplified three-state description, i.e., the classical secondary structures. More precise and complete description of protein backbone conformation can be obtained using libraries of small protein fragments that are able to approximate every part of protein structures. These libraries, called structural alphabets (SAs), have been widely used in structure analysis field, from definition of ligand binding sites to superimposition of protein structures. SAs are also well suited to analyze the dynamics of protein structures. Here, we review innovative approaches that investigate protein flexibility based on SAs description. Coupled to various sources of experimental data (e.g., B-facto

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

<a href="/en/project/ED1.1.00%2F02.0109" target="_blank" >ED1.1.00/02.0109: Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

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

Name of the periodical

Frontiers in molecular biosciences

ISSN

2296-889X

e-ISSN

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Volume of the periodical

2

Issue of the periodical within the volume

27 May 2015

Country of publishing house

CH - SWITZERLAND

Number of pages

20

Pages from-to

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UT code for WoS article

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EID of the result in the Scopus database

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