Ontology highlight
ABSTRACT:
SUBMITTER: Ruan B
PROVIDER: S-EPMC9879998 | biostudies-literature | 2023 Jan
REPOSITORIES: biostudies-literature
Ruan Biao B He Yanan Y Chen Yingwei Y Choi Eun Jung EJ Chen Yihong Y Motabar Dana D Solomon Tsega T Simmerman Richard R Kauffman Thomas T Gallagher D Travis DT Orban John J Bryan Philip N PN
Nature communications 20230126 1
To better understand how amino acid sequence encodes protein structure, we engineered mutational pathways that connect three common folds (3α, β-grasp, and α/β-plait). The structures of proteins at high sequence-identity intersections in the pathways (nodes) were determined using NMR spectroscopy and analyzed for stability and function. To generate nodes, the amino acid sequence encoding a smaller fold is embedded in the structure of an ~50% larger fold and a new sequence compatible with two set ...[more]