Results 1 to 10 of about 4,183 (137)

Sequence-encoded differences in the conformational ensembles of CITED transcriptional activation domains impact coactivator binding. [PDF]

Protein Sci
Abstract Recent advances in predicting and modeling conformational ensembles of intrinsically disordered proteins (IDPs) have provided much needed insights into sequence‐ensemble relationships. It is thought that conservation of physicochemical properties, but not the exact identity or order of the amino acids, maintains IDP ensemble properties that ...
Do TU, Kraft EJ, Chappell GF, Parnham S, Berlow RB.   +4 more
europepmc   +2 more sources

Prediction of protein-protein interaction sites in intrinsically disordered proteins

Frontiers in Molecular Biosciences, 2022
Intrinsically disordered proteins (IDPs) participate in many biological processes by interacting with other proteins, including the regulation of transcription, translation, and the cell cycle.
Ranran Chen, Ranran Chen, Xinlu Li, Xinlu Li, Yaqing Yang, Yaqing Yang, Xixi Song, Xixi Song, Cheng Wang, Cheng Wang, Dongdong Qiao   +10 more
doaj   +3 more sources

CISP, an Intrinsically Disordered Cold-Inducible Barley Protein, Functions as a Small RNA Chaperone. [PDF]

Plant Direct
ABSTRACT Low temperatures are a major environmental stress that limits plant growth and development. Understanding the molecular mechanism of cold tolerance is therefore essential for improving crop performance through molecular breeding. In this study, we focused on CISP, a small, previously uncharacterized protein, specifically induced in barley ...
Okumura Y, Haque MM, Kidou SI.
europepmc   +2 more sources

The Polymers of Life: Exploring Cellular Function Through Polymer Concepts. [PDF]

Adv Sci (Weinh)
Biomolecular phase separation reveals that a hidden layer of cellular organization is governed by the principles of polymer science. This review bridges polymer physics and cell biology, offering a primer on fundamental concepts, proposing a framework for interrogating cellular function, and synthesizing biophysical methods for decoding macromolecular ...
Chen M, Chilkoti A.
europepmc   +2 more sources

Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins

Biomolecules, 2018
Intrinsically disordered proteins (IDPs) are often modeled using ideas from polymer physics that suggest they smoothly explore all corners of configuration space.
Sharonda J. LeBlanc, Prakash Kulkarni, Keith R. Weninger   +2 more
doaj   +3 more sources

Comprehensive Biophysical Profiling Evidences Self-Oligomerization of Bacterially Expressed Pc Protein. [PDF]

Chembiochem
Polycomb (Pc), a core component of Polycomb Repressive Complex 1 (PRC1), is largely intrinsically disordered yet forms buffer‐ and concentration‐dependent higher‐order assemblies. Integrative biophysical analysis and cryo‐electron microscopy reveal dynamic, heterogeneous oligomers, whereas AlphaFold modeling suggests that structural organization is ...
Zahid M, Prajapati S, Alamdari G, Tittmann K, Kara S.   +4 more
europepmc   +2 more sources

Accurate Generation of Conformational Ensembles for Intrinsically Disordered Proteins with IDPFold [PDF]

Advanced Science
Intrinsically disordered proteins (IDPs) play pivotal roles in various biological functions whose dynamic structures are closely associated with many human diseases, including cancer, diabetes, and Alzheimer disease.
Junjie Zhu, Zhengxin Li, Zhuoqi Zheng, Bo Zhang, Bozitao Zhong, Jie Bai, Xiaokun Hong, Taifeng Wang, Ting Wei, Jianyi Yang, Hai‐Feng Chen   +10 more
doaj   +2 more sources

idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R

PLoS ONE, 2022
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are proteins or protein-domains that do not have a single native structure, rather, they are a class of flexible peptides that can rapidly adopt multiple conformations ...
William M. McFadden, Judith L. Yanowitz
doaj   +3 more sources

Prediction of folding patterns for intrinsic disordered protein

Scientific Reports, 2023
The conformation flexibility of natural protein causes both complexity and difficulty to understand the relationship between structure and function. The prediction of intrinsically disordered protein primarily is focusing on to disclose the regions with ...
Jiaan Yang, Wen-xiang Cheng, Gang Wu, Sitong Sheng, Peng Zhang   +4 more
doaj   +1 more source

Identification of ligand binding sites in intrinsically disordered proteins with a differential binding score

Scientific Reports, 2021
Screening ligands directly binding to an ensemble of intrinsically disordered proteins (IDP) to discover potential hits or leads for new drugs is an emerging but challenging area as IDPs lack well-defined and ordered 3D-protein structures.
Qiao-Hong Chen, V. V. Krishnan
doaj   +1 more source