首页> 外文期刊>Chemistry: A European journal >Peptide Recognition:Encapsulation and alpha-Helical Folding of a Nine-Residue Peptide within a Hydrophobic Dimeric Capsule of a Bowl-Shaped Host
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Peptide Recognition:Encapsulation and alpha-Helical Folding of a Nine-Residue Peptide within a Hydrophobic Dimeric Capsule of a Bowl-Shaped Host

机译:肽识别:碗形宿主疏水二聚体胶囊中的九个残基肽的封装和α-螺旋折叠。

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摘要

A dimeric capsule of coordination bowl 1 encapsulated a nine-residue peptide (Trp-Ala-Glu-Ala-Ala-Ala-Glu-Ala-Trp;2) within the large hydrophobic cavity in water,and stabilized the alpha-helical conformation of bound 2.An NMR titration experiment revealed that monomeric bowl 1 recognized two Trp residues at the both terminals of 2 through 1/2=1:1 to 2:1 complexation.The 1:1 and 2:1 species exist in equilibrium even in the presence of excess 1.It was found that the formation of the 2:1 complex,in which two bowls of 1 wrapped the whole of 2,became dominant by the addition of NaNO_3 due to the fact that the enhanced ion strength increased the hydrophobic interaction between Trp residues and the cavity of 1.The alpha-helical conformation of 2 within the dimeric capsule of 1 was elucidated from detailed NOESY analysis.
机译:配位碗1的二聚体胶囊将9个残基的肽(Trp-Ala-Glu-Ala-Ala-Ala-Glu-Ala-Trp; 2)包裹在水中的大疏水腔中,并稳定了其的α-螺旋构象结合2的NMR滴定实验表明,单体碗1在2到1/2 = 1:1到2:1络合的两个末端都识别出两个Trp残基。即使在存在过量的1。发现形成2:1的络合物,其中两碗1包裹了整个2,由于加入了NaNO_3而占优势,这是由于增强的离子强度增加了疏水性Trp残基和1的腔之间的相互作用。详细的NOESY分析阐明了1的二聚体胶囊中2的α-螺旋构象。

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