Abstract
The surface labeling methods introduced in this chapter are designed to provide information regarding the relative orientation of the protein molecules in large protein complexes. Such information is often required in case the common X-ray crystallography fails to produce results for the whole complex, e.g., because crystals of suitable quality cannot be obtained for the whole complex, but for its individual components. These methods are also used to support the interpretation of high-resolution electron micrographs. This chapter focuses on the most common technique, the attachment of a chemical linker to certain amino acid residues and mass spectrometric mapping of binding or non-binding to putative or unknown protein interaction surfaces (Fig. 14.1).
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© 2009 Springer-Verlag Berlin Heidelberg
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Nölting, B. (2009). Surface labeling analysis of protein interactions. In: Methods in Modern Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-03022-2_14
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DOI: https://doi.org/10.1007/978-3-642-03022-2_14
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Online ISBN: 978-3-642-03022-2
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