Structural Divergence Exceeds Sequence Divergence for a Family of Intrinsically Disordered Proteins
نویسندگان
چکیده
منابع مشابه
Improving Sequence Alignments For Intrinsically Disordered Proteins
Here we analyze sequence alignments for intrinsically disordered proteins. For 55 disordered protein families we measure the performance of different scoring matrices and propose one adjusted to disordered regions. An iterative algorithm of realigning sequences and recalculating matrices is designed and tested. For each matrix we also test a wide range of gap penalties. Results show an improvem...
متن کاملKMAD: knowledge-based multiple sequence alignment for intrinsically disordered proteins
UNLABELLED Intrinsically disordered proteins (IDPs) lack tertiary structure and thus differ from globular proteins in terms of their sequence-structure-function relations. IDPs have lower sequence conservation, different types of active sites and a different distribution of functionally important regions, which altogether make their multiple sequence alignment (MSA) difficult. The KMAD MSA soft...
متن کاملDescribing sequence-ensemble relationships for intrinsically disordered proteins.
Intrinsically disordered proteins participate in important protein-protein and protein-nucleic acid interactions and control cellular phenotypes through their prominence as dynamic organizers of transcriptional, post-transcriptional and signalling networks. These proteins challenge the tenets of the structure-function paradigm and their functional mechanisms remain a mystery given that they fai...
متن کاملIntrinsically 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 ...
متن کاملIntrinsically Disordered Proteins
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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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2013
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2012.11.339