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Title
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Secondary structure and topology of Acanthamoeba profilin I as determined by heteronuclear nuclear magnetic resonance spectroscopy.
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Authors
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S.J.Archer,
V.K.Vinson,
T.D.Pollard,
D.A.Torchia.
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Ref.
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Biochemistry, 1993,
32,
6680-6687.
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PubMed id
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Abstract
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The protein profilin binds to both actin and the head groups of
poly)phosphoinositide)s and may regulate both actin assembly and the
phosphoinositide signaling pathway. As a first step in understanding the
activity of profilin at the molecular level, we have determined the secondary
structure of Acanthamoeba profilin I in solution using multidimensional,
heteronuclear NMR spectroscopy. Using a combination of triple-resonance (1H,
13C, 15N) experiments, we obtained virtually complete backbone and side-chain
resonance assignments based solely on scalar couplings. 3D and 4D NOESY
experiments were then used to determine the secondary structure and global fold
of Acanthamoeba profilin I. The central feature of the protein structure is a
five-stranded antiparallel beta-sheet flanked by three helices and a short
two-stranded antiparallel beta-sheet.
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