Comparative analysis of ¹³C chemical shifts of β-sheet amyloid proteins and outer membrane proteins.

ABSTRACT: Cross-β amyloid fibrils and membrane-bound β-barrels are two important classes of β-sheet proteins. To investigate whether there are systematic differences in the backbone and sidechain conformations of these two families of proteins, here we analyze the ¹³C chemical shifts of 17 amyloid proteins and 7 β-barrel membrane proteins whose high-resolution structures have been determined by NMR. These 24 proteins contain 373 β-sheet residues in amyloid fibrils and 521 β-sheet residues in β-barrel membrane proteins. The ¹³C chemical shifts are shown in 2D ¹³C-¹³C correlation maps, and the amino acid residues are categorized by two criteria: (1) whether they occur in β-strand segments or in loops and turns; (2) whether they are water-exposed or dry, faci

SUBMITTER: Somberg NH 

PROVIDER: S-EPMC8828358 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature