Efficient Stereospecific H^β2/3 NMR Assignment Strategy for Mid-Size Proteins.

ABSTRACT: We present a strategy for stereospecific NMR assignment of H^β2 and H^β3 protons in mid-size proteins (~150 residues). For such proteins, resonance overlap in standard experiments is severe, thereby preventing unambiguous assignment of a large fraction of β-methylenes. To alleviate this limitation, assignment experiments may be run in high static fields, where higher decoupling power is required. Three-bond H^α-H^β J-couplings (³ J _Hα-Hβ) are critical for stereospecific assignments of β-methylene protons, and for determining rotameric χ₁ states. Therefore, we modified a pulse sequence designed to measure accurate ³ J _Hα-Hβ couplings such that probe heating was reduced, while the dec

SUBMITTER: Born A 

PROVIDER: S-EPMC6513325 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature