Question

17) Consider the following experimental methods that are commonly used in biochemistry: A) dynamic light scattering. B) polycrylamide gel electrophoresis (PAGE) with SDS present. C) polycrylamide gel electrophoresis (PAGE) without SDS present. D) surface plasmon resonance (SPR) E) differential scanning fluorimetry (DSF) F) analytical ultracentrifugation (equilibrium type) G) gel filtration chromatography (a) Which three of the methods are best for providing an estimate of the molecular weight of a protein in solution, in its native (non-denatured) form? (3 pts) Write the letters corresponding to 3 best choices here: (b) Which one of the methods is likely to provide the most accurate molecular weight of a protein in solution, in its native (non-denatured) form? (2 pts Write the letter corresponding to one best choice here: 18) An SPR trace for a ligand binding to a protein is shown below. RU (a) State appropriate units for the horizontal axis. (2 pts) (b) What is happening when the trace is slowly rising (the part of the curve marked with #. (2 pts)

Answer 1

1) Three methods that can be used to determine the molecular weight of a protein in its native form-

C) PAGE without SDS

F) analytical ultracentrifugation

G) Gel Filtration chromatography

2) Gel filtration

3) a) X axis = Time (seconds)

b) The trace is rising means that the ligand is binding to the protein