FRET is a widely used biophysical technique for the characterization of a wide range of biomolecular interactions. Give a brief description of how a FRET experiement is done.
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FRET is a widely used biophysical technique for the characterization of a wide range of biomolecular interactions. Give a brief description of how a FRET experiement is done.
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- SPR is one of many techniques to examine binding affinities of biomolecules. Choose another technique that can be used to measure binding affinity between two biomolecules, and briefly compare and contrast this technique with SPR. (Hint: think about sample requirements, the type of data produced, potential pitfalls with the techniques, etc.)Describe the principal biophysical and biochemical techniques used to study tertiary and quaternary structure of proteins.Identify the selected functional groups inside of the red dotted lines.
- Give other chromatographic techniques that can be used for separating non-polar biomolecules, such as lipids. Explain the principle in terms of lipid separation.briefly explain the physical mechanism by which amino acids are separated during paper chromatography.Two common methods of denaturing proteins in the lab are to increase the temperature and/or add chemical denaturants like the detergent SDS (shown below). Describe how each of these processes (heating and addition of SDS) disrupts the forces and interactions that stabilize the native state, leading to unfolding. The answer should include a discussion of the Gibbs free energy of folding, enthalpy, and entropy.