5.1 The Z domain scaffoldThe work i

5.1 The Z domain scaffold

The work in this thesis is based on the immunotechnological use of affinity ligands

(denoted affibodies) selected from protein libraries based on the so-called Z domain,

utilized as scaffold for library constructions. This Z domain is a 58 aa non-cystein

protein consisting of three anti-parallel α-helices forming a bundle structure. The Z

domain corresponds to an engineered variant of the native B domain of

staphylococcal protein A, in which an Asn28-Gly29 dipeptide sequence, sensitive to

fusion protein cleavage by hydroxylamine, has been changed into an Asn-Ala

sequence. In addition, an alanine residue at position one has been changed into a

valine (Nilsson et al., 1987). This Z domain has been frequently used as affinity

fusion partner for the production of either Z or ZZ-fusion proteins in a number of

different host cells (

Kết quả (Trung) 1:

5.1 Z-domain scaffolding work in this paper based immunotechnological affinity ligands used in the so-called Z-based domain selection (referred to as pro and body) from the protein library use as scaffold library construction. The Z-domain is 58 aa non - cysteine ​​protein consisting three antiparallel α-helix formation bouquet structure. Z domain corresponding B-domain works of the machine deformation Staphylococcus aureus protein A, which Asn28 Gly29 dipeptide sequences on sensitive Asn Ala, became a hydroxylamine, a fusion protein rupture sequences. Further, at a position to alanine residues valine (Nielsen et al., 1987). This domain is often used as an affinity Z Z or ZZ fusion protein produced in large amounts of fusion partner in different host cells (

Kết quả (Trung) 3:

5.1 Z域支架

本文的工作是基于亲和配体的

immunotechnological使用（表示affibodies）选自基于所谓的Z结构域蛋白库，

作为图书馆建筑脚手架。这是一个58个氨基酸的Z域非半胱氨酸

蛋白由三个反平行α螺旋形成一束结构。Z

域对应于一个设计的变体的本土的B结构域的

金黄色葡萄球菌A蛋白，其中一个asn28-gly29二肽序列，敏感的

融合蛋白裂解羟胺，已经变成了一个天冬酰胺丙氨酸

序列。此外，一个丙氨酸残基在位置已改为

缬氨酸（尼尔森等人。，1987）。该Z域已被经常使用的亲和

融合的合作伙伴生产的Z或ZZ融合蛋白在一些

不同宿主细胞（