中文摘要：

从中国鸟蜘蛛 Ornithoctonus huwena 净化的 Huwentoxin-XI 是有两项反朊酶活动和钾隧道堵住活动的毒素。决定它的解决方案结构， huwentoxin-XI 在酵母被表示真核细胞的表达式系统并且由 NMR 学习了。把策略标记的 15N 被用来便于回声任务的过程。质子和氮回声的将近完全的顺序特定的任务被分析获得一系列二维(2D ) 并且三维(3D ) 系列，包括 DQF 舒适， TOCSY， NOESY， 15N-1H HSQC， 15N-1H HNHA， 15N-1H HNHB， 15N-1H TOCSY-HSQC 和 15N-1H NOESY-HSQC 系列。huwentoxin-XI 的第二等的结构分析证明它主要从 Gln45 从 Thr3 包含 N 终端 310 螺旋到 Arg5 和一个 C 终端 alpha 螺旋到 Cys52，加 Glu18-Asn23， Thr26-Ile31 和 Asn40-Lys41 的一张搁浅三元组的反平行的贝它表。这些研究为 huwentoxin-XI 的最后的结构决心提供一个稳固的基础。

英文摘要：

Huwentoxin-XI purified from the Chinese bird spider Ornithoctonus huwena is a toxin with both antiprotease activity and potassium channel blocking activity. To determine its solution structure, huwentoxin-XI was expressed in a yeast eukaryotic expression system and studied by NMR. The ^15N labeling strategy was used to facilitate the process of resonance assignments. The nearly complete sequence-specific assignments of proton and nitrogen resonances were obtained by analyzing a series of two-dimensional （2D） and three-dimensional （3D） spectra, including DQF-COSY, TOCSY, NOESY, ^15N-^1H HSQC, ^15N-^1H HNHA, ^15N-^1H HNHB, ^15N-^1H TOCSY-HSQC and ^15N-^1H NOESY-HSQC spectra. Secondary structure analysis of huwentoxin-XI showed that it mainly contains an N-terminal 310-helix from Thr3 to Arg5 and a C-terminal α-helix from Gln45 to Cys52, plus a triple-stranded antiparallel β-sheet of Glu18-Asn23, Thr26-Ile31 and Asn40-Lys41. These studies provide a solid basis for the final structure determination of huwentoxin-XI.