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Computational Prediction of Intrinsically Disordered Proteins Based on Protein Sequences and Convolutional Neural Networks.
Comput Intell Neurosci
January 2022
School of Computer Science and Technology, Tiangong University, Tianjin 300387, China.
Intrinsically disordered proteins (IDPs) possess at least one region that lacks a single stable structure in vivo, which makes them play an important role in a variety of biological functions. We propose a prediction method for IDPs based on convolutional neural networks (CNNs) and feature selection. The combination of sequence and evolutionary properties is used to describe the differences between disordered and ordered regions.
View Article and Find Full Text PDFIntrinsic disorder-based design of stable globular proteins.
Prog Mol Biol Transl Sci
June 2021
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. Electronic address:
Directed stabilization of globular proteins via substitution of a minimal number of amino acid residues is one of the most complicated experimental tasks. In this work, we have successfully used algorithms for the evaluation of intrinsic disorder predisposition (such as PONDR® FIT and IsUnstruct) as tools for searching for the weakened regions in structured globular proteins. We have shown that the weakened regions found by these programs as regions with highest levels of predicted intrinsic disorder predisposition are a suitable target for introduction of stabilizing mutations.
View Article and Find Full Text PDFIntrinsic Disorder-Based Design of Stabilizing Disulphide Bridge in Gαo Protein.
Protein Pept Lett
October 2016
Institute of Protein Research (Moscow office), Room 104, Vavilova Street 34, Moscow, GSP 1, 117334, Russia.
In this study, we have used an approach that allows us to determine in what region of the polypeptide chain of protein it is required to insert a disulphide bond in order to stabilize it. In our previous paper [Melnik et al., JBSD.
View Article and Find Full Text PDFHow Common Is Disorder? Occurrence of Disordered Residues in Four Domains of Life.
Int J Mol Sci
August 2015
Institute of Protein Research, Russian Academy of Sciences, Pushchino 142290, Moscow Region, Russia.
Disordered regions play important roles in protein adaptation to challenging environmental conditions. Flexible and disordered residues have the highest propensities to alter the protein packing. Therefore, identification of disordered/flexible regions is important for structural and functional analysis of proteins.
View Article and Find Full Text PDFIsUnstruct: prediction of the residue status to be ordered or disordered in the protein chain by a method based on the Ising model.
J Biomol Struct Dyn
October 2013
a Institute of Protein Research of the Russian Academy of Sciences, 4 Institutskaya str., Pushchino , Moscow Region , 142290 , Russia.
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