Speaker: R. Andrew Byrd, Structural Biophysics Laboratory, Program in Structural Biology, Division of Basic Sciences, National Cancer Institute, Frederick, MD

Topic: NMR in Structural Biology and the Interface with Mass Spectrometry

Place: Building 426, Conference Room, NCI-Frederick, Frederick, MD

Time: Tuesday, October 19, 1999, at 1:30 PM

Abstract: Modern NMR methods are very powerful in providing atomic resolution structural, dynamic, and interaction information for macromolecules. The key element in opening up NMR to the study of macromolecular structure determination and investigation of complexes has been the use of stable isotope labeling (e.g. ¹³C, ¹⁵N, and ²H). The labeling takes many forms ranging from uniform to residue specific or even moiety specific (e.g. the protonation of methyl groups in an otherwise completely deuterated protein). While the actual task of labeling is handled biosynthetically, the monitoring of the labeling and the identity and characterization of the proteins are best achieved by mass spectrometry. We utilize HPLC-electrospray mass spectrometry to perform these tasks on a wide range of samples. The talk will review the NMR needs and place them in the context of the biosynthetic schemes. Examples of the types and uses of mass spectrometry will be covered to illustrate the symbiosis of this use of mass spectrometry with NMR in structural biology studies.