Core mutants of the immunoglobulin binding domain of streptococcal protein G: Stability and structural integrity
نویسندگان
چکیده
منابع مشابه
Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G.
The folding of the small (56 residues) highly stable B1 immunoglobulin binding domain (GB1) of streptococcal protein G has been investigated by quenched-flow deuterium-hydrogen exchange. This system represents a paradigm for the study of protein folding because it exhibits no complicating features superimposed upon the intrinsic properties of the polypeptide chain. Collapse to a semicompact sta...
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BACKGROUND Half-life extension strategies have gained increasing interest to improve the pharmacokinetic and pharmacodynamic properties of protein therapeutics. Recently, we established an immunoglobulin-binding domain (IgBD) from streptococcal protein G (SpGC3) as module for half-life extension. SpGC3 is capable of binding to the Fc region as well as the CH1 domain of Fab arms under neutral an...
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Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular replacement, based on the structure of the B2 domain (Brookhaven accession code 1PGX). Final R values are 0.174 and 0.198 for orthorhombic and trigonal forms, for diffraction data from 6.0 to 2.07 A and...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1996
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(96)01262-8