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 (Anh) 1:

5.1 The Z domain scaffoldThe work in this thesis is based on the immunotechnological use of affinity ligands(denoted affibodies) selected from the protein libraries based on the so-called Z-domain,utilized as scaffold for library constructions. This Z domain is a 58 a a non-cysteineprotein consisting of three anti parallel Alpha-helicenes habit-forming a bundle with structure. The Zdomain corresponds to an engineered variant of the native B domain ofstaphylococcal protein A, in which an Asn28-Gly29 dipeptide sequence, sensitive tofusion protein cleavage by hydroxylamine, has been changed into an Asn-Alasequence. In addition, an alanine residue at position one has been changed into avaline (Nilsson et al., 1987). This Z domain has been frequently used as affinityfusion partner for the production of either Z or ZZ-fusion proteins in a number ofdifferent host cells (

Kết quả (Anh) 2:

5.1 The Z domain scaffold The work in this thesis is based on the use of affinity ligands immunotechnological (denoted affibodies) selected from libraries based on the comparison of protein-gọi Z domain, utilized as scaffold for library constructions. This domain Z is a non-cysteine ​​58 aa protein consisting of three α-helices anti-parallel structure forming a bundle. The Z domain corresponds to safety engineered variant of the native B domain of staphylococcal protein A, Asn28-Gly29 security chứa dipeptide sequence, sensitive to the fusion protein cleavage by hydroxylamine, đã changed Asn-Ala Security Into sequence. In addition, police alanine residue at position one đã changed Into a valine (Nilsson et al., 1987). This domain Z Đã USED thường as affinity fusion partner for the production of hoặc Z ZZ-fusion proteins or in a number of khác host cells (