0431519 - ÚOCHB 2015 DE eng J - Journal Article
Prosser, C. E. - Waters, L. C. - Muskett, F. W. - Veverka, Václav - Addis, P. W. - Griffin, L. M. - Baker, T. S. - Lawson, A. D. G. - Wernery, U. - Kinne, J. - Henry, A. J. - Taylor, R. J. - Carr, M. D.
N-15, C-13 and H-1 resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
Biomolecular NMR Assignments. Roč. 8, č. 1 (2014), s. 113-116. ISSN 1874-2718. E-ISSN 1874-270X
Institutional support: RVO:61388963
Keywords : heavy chain antibody * VHH * NMR resonance assignments
Subject RIV: CE - Biochemistry
Impact factor: 0.760, year: 2014

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 N-15, C-13 and H-1 assignments for a free VHH. Analysis of the backbone chemical shift data obtained indicates that the VHH is comprised predominantly of beta-sheets corresponding to nearly 60 % of the protein backbone.
Permanent Link: http://hdl.handle.net/11104/0236182