Secondary Structure Prediction for Intrinsically Disordered Proteins
نویسندگان
چکیده
منابع مشابه
Intrinsically disordered proteins.
Our understanding of protein function has been predominated by the view that proteins need to adopt a defined three dimensional structure to be able to carry out their function. Indeed, crystal structures of numerous proteins have been instrumental in establishing the structure– function paradigm. For example, the structures of numerous enzymes have highlighted the need for particular chemical ...
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Intrinsically disordered proteins (IDPs) partially or completely lack a cooperatively folded structure under native conditions, preventing their equilibrium state from being adequately described by a single structural model. Reaching the goal of quantitatively describing IDP structure–function relationships has required the development of novel experiments aiming to characterize their structure...
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In the same way that neither a messy lab bench nor a clean one is a reliable indicator of a researcher’s productivity, a protein’s function cannot be judged solely on the basis of its neatly folded and stable domains. As evidenced by recent work discussed in this Select, we are learning that intrinsically disordered regions feature in many of the cell’s most productive multitaskers, proteins wh...
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Intrinsically disordered proteins (IDPs) have the potential to play a unique role in the study of proteins and the relationships between structure and function. Intrinsic disorder affects chemical and cellular events such as cell signaling, macromolecular self-assembly, protein removal and crystal nucleation and growth. This chapter explores the structural principles by which IDPs act and revea...
متن کاملConstructing ensembles for intrinsically disordered proteins.
The relatively flat energy landscapes associated with intrinsically disordered proteins makes modeling these systems especially problematic. A comprehensive model for these proteins requires one to build an ensemble consisting of a finite collection of structures, and their corresponding relative stabilities, which adequately capture the range of accessible states of the protein. In this regard...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2020
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2019.11.1272