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- W2061885536 abstract "GlgS is a 7892-Da protein which is involved in glycogen biosynthesis in bacteria. We report the 1H, 15N and 13C NMR assignments of the backbone and side-chain resonances at 25 degrees C and pH 6.7 from two-dimensional homonuclear and three-dimensional heteronuclear NMR experiments. The secondary structure of the protein was determined using sequential and medium-range NOE correlations, vicinal 3J(NH-H alpha) coupling values and amide proton exchange rates. The secondary structure obtained is consistent with the secondary chemical shifts of 1H alpha, 13C alpha and 13C = O. It was found that the secondary structure of GlgS comprises two amphipathic helices (Asn10-Met21 and Glu39-Arg60), one short highly hydrophobic helix (Ile30-Val33), a short extended beta-strand-like fragment (Arg26-Asp29) and two type I beta-turns (His22-Gly25 and Thr34-Met37). An overall topology of GlgS is suggested based on long-range NOEs. The elements of secondary structure form a sandwich in which the beta-strand and the short hydrophobic helix are positioned between the two amphipathic helices." @default.
- W2061885536 created "2016-06-24" @default.
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- W2061885536 date "1997-06-01" @default.
- W2061885536 modified "2023-10-17" @default.
- W2061885536 title "1H, 15N and 13C NMR Assignments, Secondary Structure and Overall Topology of the Escherichia Coll Glgs Protein" @default.
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- W2061885536 doi "https://doi.org/10.1111/j.1432-1033.1997.t01-1-00301.x" @default.
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