MoRFPred-plus: Computational Identification of MoRFs in Protein Sequences using Physicochemical Properties and HMM profiles.

Journal: Journal of theoretical biology

Published Date: Jan 21, 2018

Abstract

MOTIVATION: Intrinsically Disordered Proteins (IDPs) lack stable tertiary structure and they actively participate in performing various biological functions. These IDPs expose short binding regions called Molecular Recognition Features (MoRFs) that permit interaction with structured protein regions. Upon interaction they undergo a disorder-to-order transition as a result of which their functionality arises. Predicting these MoRFs in disordered protein sequences is a challenging task.

Authors

Ronesh Sharma
Maitsetseg Bayarjargal

Department of Health Science, Fiji National University, Fiji.
Tatsuhiko Tsunoda

Center for Integrative Medical Sciences, RIKEN Yokohama, Yokohama, 230-0045, Japan. tatsuhiko.tsunoda@riken.jp.
Ashwini Patil

Human Genome Center, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan. ashwini@hgc.jp.
Alok Sharma

Center for Integrative Medical Sciences, RIKEN Yokohama, Yokohama, 230-0045, Japan.

Keywords

Algorithms Amino Acid Sequence Binding Sites Computational Biology Intrinsically Disordered Proteins Models, Theoretical Protein Binding Protein Domains Support Vector Machine

External Resources

View on PubMed Access via DOI PubMed (29042212)

MoRFPred-plus: Computational Identification of MoRFs in Protein Sequences using Physicochemical Properties and HMM profiles.

Abstract

Authors

Keywords

External Resources

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