Results 301 to 310 of about 7,902,914 (332)

Intrinsically disordered protein regions at membrane contact sites

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2021
Membrane contact sites (MCS) are regions of close apposition between membrane-bound organelles. Proteins that occupy MCS display various domain organisation. Among them, lipid transfer proteins (LTPs) frequently contain both structured domains as well as regions of intrinsic disorder.
Denisa, Jamecna, Bruno, Antonny
openaire   +2 more sources

Intrinsically Disordered Proteins and Structured Proteins With Intrinsically Disordered Regions Have Different Functional Roles in the Cell

PLoS ONE, 2019
Abstract Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Sergio Forcelloni, Andrea Giansanti
exaly   +5 more sources

Introduction to Intrinsically Disordered Proteins and Regions

Intrinsically Disordered Proteins, 2019
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are fascinating dynamic conformational ensembles that are observed under physiological conditions. They facilitate a wide variety of biological processes via mechanisms that are distinct from their structured counterparts.
Alan Keith Dunker, Christopher J Oldfield, Vladimir Uversky   +2 more
exaly   +3 more sources

Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Annual Review of Biochemistry, 2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between ...
Christopher J, Oldfield, A Keith, Dunker
openaire   +2 more sources

Prediction of the Disordered Regions of Intrinsically Disordered Proteins Based on the Molecular Functions

Protein & Peptide Letters, 2020
Background: Intrinsically disordered proteins lack a well-defined three dimensional structure under physiological conditions while possessing the essential biological functions. They take part in various physiological processes such as signal transduction, transcription and posttranslational modifications and etc.
WeiXia, Xie, Yong E, Feng
openaire   +2 more sources

Functional Roles of Transiently and Intrinsically Disordered Regions Within Proteins

FEBS Journal, 2015
Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well‐folded structures. Even small, well‐folded single‐domain proteins are structurally heterogeneous and contain multiple foldon units with different conformational stability ...
Vladimir Uversky
exaly   +4 more sources

ProtSSSD: A Novel Approach for Intrinsically Disordered Protein Region Prediction Using Protein Language Model

IEEE International Conference on Bioinformatics and Biomedicine
Determining the intrinsically disordered regions of proteins is crucial for elucidating their biological functions and the mechanisms of related diseases.
Lei Wang, Zi-Lu Zeng, Yan Wang, Zhi-Dong Xue   +3 more
semanticscholar   +1 more source

DeepIDP-2L: protein intrinsically disordered region prediction by combining convolutional attention network and hierarchical attention network

Bioinform., 2021
MOTIVATION Intrinsically disordered regions (IDRs) are widely distributed in proteins. Accurate prediction of IDRs is critical for the protein structure and function analysis.
Yi-Jun Tang, Yi-He Pang, Bin Liu
semanticscholar   +1 more source

Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof.

Emerging Topics in Life Sciences, 2020
Intrinsically disordered protein regions (IDRs) - regions that do not fold into a fixed three-dimensional structure but instead exist in a heterogeneous ensemble of conformations - have recently entered mainstream cell biology in the context of liquid ...
Erik W. Martin, A. Holehouse
semanticscholar   +1 more source

An intrinsically disordered protein in F127 hydrogel: Fluorescence correlation spectroscopy and structural diversity of beta casein

, 2021
Intrinsically Disordered Proteins (IDPs) switch between diverse structures which prevents them from crystallization. FCS of the IDP beta casein (β-CN), labeled with Alexa488, suggests that in buffer the structure fluctuates between a highly extended ...
Ushasi Pramanik, Subhajit Chakraborty, K. Bhattacharyya, S. Mukherjee   +3 more
semanticscholar   +1 more source