Solution structure of an atypical WW domain in a novel β-clam-like dimeric form
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چکیده
منابع مشابه
Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus.
A new protein expression vector design utilizing an N-terminal six-histidine tag and tobacco etch virus protease cleavage site upstream of the hepatitis C virus NS5A sequence has resulted in a more straightforward purification method and improved yields of purified NS5A domain I protein. High-resolution diffracting crystals of NS5A domain I (amino acids 33 to 202) [NS5A(33-202)] were obtained b...
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Protein folding barriers result from a combination of factors including unavoidable energetic frustration from nonnative interactions, natural variation and selection of the amino acid sequence for function, and/or selection pressure against aggregation. The rate-limiting step for human Pin1 WW domain folding is the formation of the loop 1 substructure. The native conformation of this six-resid...
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The solid-state structure of a dimeric β-diketiminate magnesium(II) complex is discussed. The compound, di-μ-iodido-bis-[(-{4-amino-1,5-bis-[2,6-bis-(propan-2-yl)phen-yl]pent-3-en-2-yl-idene}aza-nido-κ2N,N')magnesium(II)] toluene sesquisolvate, [Mg2(C29H41N2)2I2]·1.5C7H8, crystallizes as two independent mol-ecules, each with 2/m crystallographic site symmetry, located at Wyckoff sites 2c and 2d...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2007
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2007.01.008