6x1k
From Proteopedia
Solution NMR structure of de novo designed TMB2.3
Structural highlights
Publication Abstract from PubMedTransmembrane beta-barrel proteins (TMBs) are of great interest for single-molecule analytical technologies because they can spontaneously fold and insert into membranes and form stable pores, but the range of pore properties that can be achieved by repurposing natural TMBs is limited. We leverage the power of de novo computational design coupled with a "hypothesis, design, and test" approach to determine TMB design principles, notably, the importance of negative design to slow beta-sheet assembly. We design new eight-stranded TMBs, with no homology to known TMBs, that insert and fold reversibly into synthetic lipid membranes and have nuclear magnetic resonance and x-ray crystal structures very similar to the computational models. These advances should enable the custom design of pores for a wide range of applications. De novo design of transmembrane beta barrels.,Vorobieva AA, White P, Liang B, Horne JE, Bera AK, Chow CM, Gerben S, Marx S, Kang A, Stiving AQ, Harvey SR, Marx DC, Khan GN, Fleming KG, Wysocki VH, Brockwell DJ, Tamm LK, Radford SE, Baker D Science. 2021 Feb 19;371(6531). pii: 371/6531/eabc8182. doi:, 10.1126/science.abc8182. PMID:33602829[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|