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Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

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Updated: Feb 4, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Predicting Functions of Disordered Proteins with MoRFpred.

Christopher J Oldfield¹, Vladimir N Uversky^2,3, Lukasz Kurgan⁴

¹Department of Computer Science, Virginia Commonwealth University, Richmond, VA, USA.

Methods in Molecular Biology (Clifton, N.J.)

|October 10, 2018

Summary

This summary is machine-generated.

This study introduces MoRFpred, a web server for accurately predicting molecular recognition features (MoRFs) in intrinsically disordered proteins. Understanding MoRFs is crucial for various cellular processes and protein interactions.

Keywords:

Intrinsic disorder MoRFpred MoRFs Molecular recognition features Prediction Protein-protein interactions

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A Protocol for Computer-Based Protein Structure and Function Prediction

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Area of Science:

Biochemistry
Bioinformatics
Computational Biology

Background:

Intrinsically disordered proteins (IDPs) and regions (IDRs) play vital roles in cellular functions, particularly in mediating protein-protein interactions.
Molecular recognition features (MoRFs) are specific segments within IDRs that undergo a disorder-to-order transition upon binding to partner proteins.
MoRFs are implicated in essential biological processes including translation, cellular transport, signal transduction, and regulation across all life domains.

Purpose of the Study:

To describe MoRFpred, a computational tool for the accurate prediction of MoRFs in protein sequences.
To provide instructions on using the MoRFpred web server and interpreting its output.
To demonstrate the practical application of MoRFpred through case studies, highlighting the significance of evolutionary conservation in MoRF regions.

Main Methods:

Development and implementation of the MoRFpred computational tool.
Creation of a user-friendly web server for MoRFpred accessibility.
Utilizing case studies to analyze the evolutionary conservation patterns of predicted MoRFs.

Main Results:

MoRFpred demonstrates high accuracy in identifying MoRFs within intrinsically disordered protein sequences.
The MoRFpred web server offers a practical and accessible platform for researchers to predict MoRFs.
Case studies illustrate the importance of evolutionary conservation as a feature for validating MoRF predictions.

Conclusions:

MoRFpred is a valuable resource for the accurate prediction and analysis of MoRFs.
The web server facilitates the study of intrinsically disordered proteins and their roles in molecular recognition.
Understanding MoRFs and their conservation aids in elucidating protein function and regulatory mechanisms.