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

被引：0
作者：
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
机构：
[1] University of Leicester,Department of Biochemistry, Henry Wellcome Building
[2] UCB,undefined
[3] Central Veterinary Research Laboratory,undefined
来源：
Biomolecular NMR Assignments | 2014年 / 8卷
关键词：
Heavy chain antibody; VHH; NMR resonance assignments; Secondary structure;
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摘要：
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 15N, 13C and 1H 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.
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页码：113 / 116
页数：3
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