Unknown

Dataset Information

0

Computational design of membrane proteins using RosettaMembrane.


ABSTRACT: Computational membrane protein design is challenging due to the small number of high-resolution structures available to elucidate the physical basis of membrane protein structure, multiple functionally important conformational states, and a limited number of high-throughput biophysical assays to monitor function. However, structural determination of membrane proteins has made tremendous progress in the past years. Concurrently the field of soluble computational design has made impressive inroads. These developments allow us to tackle the formidable challenge of designing functional membrane proteins. Herein, Rosetta is benchmarked for membrane protein design. We evaluate strategies to cope with the often reduced quality of experimental membrane protein structures. Further, we test the usage of symmetry in design protocols, which is particularly important as many membrane proteins exist as homo-oligomers. We compare a soluble scoring function with a scoring function optimized for membrane proteins, RosettaMembrane. Both scoring functions recovered around half of the native sequence when completely redesigning membrane proteins. However, RosettaMembrane recovered the most native-like amino acid property composition. While leucine was overrepresented in the inner and outer-hydrophobic regions of RosettaMembrane designs, it resulted in a native-like surface hydrophobicity indicating that it is currently the best option for designing membrane proteins with Rosetta.

SUBMITTER: Duran AM 

PROVIDER: S-EPMC5734395 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Computational design of membrane proteins using RosettaMembrane.

Duran Amanda M AM   Meiler Jens J  

Protein science : a publication of the Protein Society 20171115 1


Computational membrane protein design is challenging due to the small number of high-resolution structures available to elucidate the physical basis of membrane protein structure, multiple functionally important conformational states, and a limited number of high-throughput biophysical assays to monitor function. However, structural determination of membrane proteins has made tremendous progress in the past years. Concurrently the field of soluble computational design has made impressive inroads  ...[more]

Similar Datasets

| S-EPMC4108999 | biostudies-literature
2024-07-05 | GSE237017 | GEO
| S-EPMC4077665 | biostudies-literature
| S-EPMC4270820 | biostudies-other
| S-EPMC64672 | biostudies-literature
| S-EPMC2843960 | biostudies-literature
| S-EPMC7328376 | biostudies-literature
| S-EPMC6327176 | biostudies-literature
| S-EPMC6168510 | biostudies-literature
| S-EPMC3977815 | biostudies-literature