Our news journalists obtained a quote from the research, "Binding promiscuity and plasticity allow IDPs to interact with multiple partners in protein interaction networks and provide important functional advantages in molecular recognition through transient protein-protein interactions. Short interaction-prone segments within IDPs, termed molecular recognition features, represent potential binding sites that can undergo disorder-to-order transition upon binding to their partners. In this review, we summarize the evidence for the importance of IDPs in plant biology and evaluate the functions associated with intrinsic disorder in five different types of plant protein families experimentally confirmed as IDPs. Functional studies of these proteins illustrate the broad impact of disorder on many areas of plant biology, including abiotic stress, transcriptional regulation, light perception, and development."
According to the news editors, the research concluded: "Based on the roles of disorder in the protein-protein interactions, we propose various modes of action for plant IDPs that may provide insight for future experimental approaches aimed at understanding the molecular basis of protein function within important plant pathways."
For more information on this research see: Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology. The Plant Cell, 2013;25(1):38-55 (see also Molecular Recognition).
Our news journalists report that additional information may be obtained by contacting X. Sun,
Keywords for this news article include: Peptides, Proteins, Amino Acids, Nanotechnology, Palmerston North, Emerging Technologies, Molecular Recognition,
Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2013, NewsRx LLC
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