Journal
BIOPHYSICAL JOURNAL
Volume 118, Issue 12, Pages 2952-2965Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2020.05.015
Keywords
-
Categories
Funding
- Research Foundation Flanders [G.0029.12]
- National Research Development and Innovation Office of Hungary [K124670, K125340, K131702]
- Spearhead grant from Vrije Universiteit Brussel, Brussels, Belgium [SRP51]
- Natural Sciences and Engineering Research Council of Canada Discovery Grant
Ask authors/readers for more resources
Intrinsically disordered proteins are proteins whose native functional states represent ensembles of highly diverse conformations. Such ensembles are a challenge for quantitative structure comparisons because their conformational diversity precludes optimal superimposition of the atomic coordinates necessary for deriving common similarity measures such as the root mean-square deviation of these coordinates. Here, we introduce superimposition-free metrics that are based on computing matrices of the C alpha-C alpha distance distributions within ensembles and comparing these matrices between ensembles. Differences between two matrices yield information on the similarity between specific regions of the polypeptide, whereas the global structural similarity is captured by the root mean-square difference between the medians of the C alpha-C alpha distance distributions of two ensembles. Together, our metrics enable rigorous investigations of structure-function relationships in conformational ensembles of intrinsically disordered proteins derived using experimental restraints or by molecular simulations and for proteins containing both structured and disordered regions.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available