BCH210H1 Lecture 12: L12 Analysis of Proteins II

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Tuesday, october 3rd, 2017 10am-11am: methods for structural analysis of proteins. Spectroscopic methods use light of wavelength of protein in solution, informing secondary structure (but not where), but mostly allow you to look at conformational changes in proteins. Proteins are dynamic, changing state during catalysis and can use spectroscopy to detect whether in folded or unfolded states: all methods can deduce 3d structure of proteins, but each have strengths and limitations. Lecture 12 outline: structural analysis of proteins, x-ray crystallography, spectroscopic methods. Analysis of protein structure: x-ray crystallography, electron microscopy (em, nuclear magnetic resonance (nmr) spectroscopy. In order to do crystallography, you have to be able to crystallize the protein. Send off frozen crystals to syncatron, but them in the high intensity x-ray beams, resulting in diffraction pattern. It"s the electrons that do the diffracting, so that"s what you"re detecting.