Work

Dynamics of Antibody Domains Studied by Solution NMR

Year: 2008

Type: book-chapter

Abstract: Information on local dynamics of antibodies is important to evaluate stability, to rationally design variants, and to clarify conformational disorders at the epitope binding sites. Such information may also be useful for improved understanding of antigen recognition. NMR can be used for characterization of local protein dynamics at the atomic level through relaxation measurements. Due to the complexity of the NMR spectra, an extensive use of this method is limited to small protein molecules, for example, antibody domains and some scFv. Here, we describe a protocol that was used to study the dynamics of an antibody domain in solution using NMR. We describe protein preparation for NMR studies, NMR sample optimization, signal assignments, and dynamics experiments.

Source: Methods in molecular biology

DOI: 10.1007/978-1-59745-554-1_29

Authors: Bang K. Vu, Joseph Walsh, Dimiter S. Dimitrov, Rieko Ishima

Institutions: National Institutes of Health, National Cancer Institute, University of Pittsburgh, Frederick National Laboratory for Cancer Research

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute

Awards: G2755035673, G6374948078