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Complete sequence-specific 1H nuclear magnetic resonance assignments for the α-amylase polypeptide inhibitor tendamistat from Streptomyces tendae

Journal of Molecular BiologyPublished 1 December 1986
Allen D. Kline, Kurt Wüthrich
Citations45
SJR quartileQ1
SJR score2.21
SNIP1.13

TL;DR

The 1H nuclear magnetic resonance (n.m.r.) spectrum of the alpha-amylase inhibitor Tendamistat was completely assigned with the use of phase-sensitive homonuclear two-dimensional n.r.

Abstract

The 1H nuclear magnetic resonance (n.m.r.) spectrum of the alpha-amylase inhibitor Tendamistat was completely assigned with the use of phase-sensitive homonuclear two-dimensional n.m.r. The assignments include the non-labile protons of the 74 amino acid residues as well as the labile protons which exchange sufficiently slowly to be observed in H2O solution. The proton chemical shifts are listed at 50 degrees C and pH 3.2, which coincides with the conditions used for the determination of the three-dimensional structure of Tendamistat.

Keywords

Materials ScienceBiochemistry, Genetics and Molecular Biology