N-15, C-13 and H-1 resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody

0431519 - ÚOCHB 2015 DE eng J - Článek v odborném periodiku
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
Institucionální podpora: RVO:61388963
Klíčová slova: heavy chain antibody * VHH * NMR resonance assignments
Kód oboru RIV: CE - Biochemie
Impakt faktor: 0.760, rok: 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.
Trvalý link: http://hdl.handle.net/11104/0236182