Distinguishing Different Hydrogen-Bonded Helices in Proteins by Efficient ¹H-Detected Three-Dimensional Solid-State NMR.

ABSTRACT: Helical structures in proteins include not only α-helices but also 3₁₀ and π helices. These secondary structures differ in the registry of the C═O···H-N hydrogen bonds, which are i to i + 4 for α-helices, i to i + 3 for 3₁₀ helices, and i to i + 5 for π-helices. The standard NMR observable of protein secondary structures are chemical shifts, which are, however, insensitive to the precise type of helices. Here, we introduce a three-dimensional (3D) ¹H-detected experiment that measures and assigns CO-H^N cross-peaks to distinguish the different types of hydrogen-bonded helices. This hCOhNH experiment combines efficient cross-polarization from CO to H^N with ¹³C, ¹⁵N, and

SUBMITTER: Medeiros-Silva J 

PROVIDER: S-EPMC10880114 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature