A lipophilicity-based energy function for membrane-protein modelling and design.

ABSTRACT: Membrane-protein design is an exciting and increasingly successful research area which has led to landmarks including the design of stable and accurate membrane-integral proteins based on coiled-coil motifs. Design of topologically more complex proteins, such as most receptors, channels, and transporters, however, demands an energy function that balances contributions from intra-protein contacts and protein-membrane interactions. Recent advances in water-soluble all-atom energy functions have increased the accuracy in structure-prediction benchmarks. The plasma membrane, however, imposes different physical constraints on protein solvation. To understand these constraints, we recently developed a high-throughput experimental screen, called dsTβL, and inferred apparent insertion energies for

SUBMITTER: Weinstein JY 

PROVIDER: S-EPMC6736313 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature