Unknown

Dataset Information

0

Information theoretic measures for quantifying sequence-ensemble relationships of intrinsically disordered proteins.


ABSTRACT: Intrinsically disordered proteins (IDPs) contribute to a multitude of functions. De novo design of IDPs should open the door to modulating functions and phenotypes controlled by these systems. Recent design efforts have focused on compositional biases and specific sequence patterns as the design features. Analysis of the impact of these designs on sequence-function relationships indicates that individual sequence/compositional parameters are insufficient for describing sequence-function relationships in IDPs. To remedy this problem, we have developed information theoretic measures for sequence-ensemble relationships (SERs) of IDPs. These measures rely on prior availability of statistically robust conformational ensembles derived from all atom simulations. We show that the measures we have developed are useful for comparing sequence-ensemble relationships even when sequence is poorly conserved. Based on our results, we propose that de novo designs of IDPs, guided by knowledge of their SERs, should provide improved insights into their sequence-ensemble-function relationships.

SUBMITTER: Cohan MC 

PROVIDER: S-EPMC7462041 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Information theoretic measures for quantifying sequence-ensemble relationships of intrinsically disordered proteins.

Cohan Megan C MC   Ruff Kiersten M KM   Pappu Rohit V RV  

Protein engineering, design & selection : PEDS 20191201 4


Intrinsically disordered proteins (IDPs) contribute to a multitude of functions. De novo design of IDPs should open the door to modulating functions and phenotypes controlled by these systems. Recent design efforts have focused on compositional biases and specific sequence patterns as the design features. Analysis of the impact of these designs on sequence-function relationships indicates that individual sequence/compositional parameters are insufficient for describing sequence-function relation  ...[more]

Similar Datasets

| S-EPMC5232785 | biostudies-literature
| S-EPMC10634935 | biostudies-literature
| S-EPMC6699093 | biostudies-literature
| S-EPMC4512920 | biostudies-literature
| S-EPMC3177054 | biostudies-literature
| S-EPMC2872267 | biostudies-literature
| S-EPMC9250585 | biostudies-literature
| S-EPMC2727479 | biostudies-literature
| S-EPMC3940659 | biostudies-literature
| S-EPMC3497802 | biostudies-literature