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Structural information involved in the interpretation of the stepwise protein folding process
Alejster, P.; Jurkowski, Wiktor; Roterman-Konieczna, I.
2012In Protein folding in silico : protein folding versus protein structure prediction
Peer reviewed
 

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Keywords :
information theory; quantity of information; bit; Ramachandran map; one-step versus two-step model
Abstract :
[en] Calculating the quantity of information present in each step of the protein folding process suggests that the multistep approach requires less information than the one-step model. Quantitative analysis reveals that the amino acids present in the polypeptide chain do not carry enough information to accurately predict the values of the angles Φ and Ψ in folded proteins. This conclusion results from comparing the amount of information carried by amino acids with the quantity of information necessary to determine Φ and Ψ, taking the complete Ramachandran map as the conformational space. It is shown that the two-step model (comprising two stages, the ES and LS) requires less information, owing to the fact that the final predictions of the angles Φ and Ψ can be based on a preexisting ES structure. Analysis based on information theory points to particular zones of the Ramachandran map that appear to play an important role in the context of protein structure prediction.
Disciplines :
Life sciences: Multidisciplinary, general & others
Author, co-author :
Alejster, P.
Jurkowski, Wiktor ;  University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB)
Roterman-Konieczna, I.
External co-authors :
yes
Language :
English
Title :
Structural information involved in the interpretation of the stepwise protein folding process
Publication date :
2012
Main work title :
Protein folding in silico : protein folding versus protein structure prediction
Publisher :
Woodhead Publishing Limited
Pages :
39-54
Peer reviewed :
Peer reviewed
Available on ORBilu :
since 11 April 2016

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