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(15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
MedLine Citation:
PMID:  23359223     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Heavy chain antibodies differ in structure to conventional antibodies lacking both the light chain and the first heavy chain constant domain (CH1). Characteristics of the antigen-binding variable heavy domain of the heavy chain antibody (VHH) including the smaller size, high solubility and stability make them an attractive alternative to more traditional antibody fragments for detailed NMR-based structural analysis. Here we report essentially complete backbone and side chain (15)N, (13)C and (1)H assignments for a free VHH. Analysis of the backbone chemical shift data obtained indicates that the VHH is comprised predominantly of β-sheets corresponding to nearly 60 % of the protein backbone.
Authors:
Christine E Prosser; Lorna C Waters; Frederick W Muskett; Vaclav Veverka; Philip W Addis; Laura M Griffin; Terry S Baker; Alastair D G Lawson; Ulrich Wernery; Jorg Kinne; Alistair J Henry; Richard J Taylor; Mark D Carr
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-29
Journal Detail:
Title:  Biomolecular NMR assignments     Volume:  -     ISSN:  1874-270X     ISO Abbreviation:  Biomol NMR Assign     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101472371     Medline TA:  Biomol NMR Assign     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Biochemistry, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester, LE1 9HN, UK, cep23@le.ac.uk.
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