Structural Studies of Immunoglobulin-Binding Domains of Streptococcal Protein G
โ Scribed by Angela M. Gronenborn; G.Marius Clore
- Book ID
- 115618319
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 449 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1058-6687
No coin nor oath required. For personal study only.
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## Abstract Structural formation of segments plays pivotal roles in protein folding and stability, but how the segment influences the structural ensemble remains elusive. We engineered two hybrid proteins by replacing the central helical segment of immunoglobulin G binding domain of streptococcal p
Streptococcal protein G is an IgG-binding receptor with a molecular weight of 63 kDa as predicted from the sequence of the corresponding gene. Here we show that a truncated recombinant protein of 23 kDa still has IgG-binding capacity and also interacts specifically with human serum albumin (HSA). Th
## Abstract The structure and dynamics of the ureaโdenatured B1 immunoglobulin binding domain of streptococcal protein G (GB1) has been investigated by multidimensional heteronuclear NMR spectroscopy. Complete ^1^H, ^15^N, and ^13^C assignments are obtained by means of sequential throughโbond corre