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Fully denaturing a protein requires unfolding the chain. In some cases two different types of denaturants are required to do this. Below is a list of chemicals and their combinations. For each one select what it will do to an antibody. Antibodies are multisubunit proteins with both intra- and inter-subunit disulfide bonds. SDS, 8M urea, and BME 8M urea and BME 1. Proteins remains native. Sodium dodecyl sulfate (SDS) 2. Partial denaturation, disulfide bonds remain intact SDS and 8M urea 3. Disulfides break, but the protein remains folded. 8M Urea 4. Full denaturation: unfolding and breakage of disulfide bonds. V Tris buffer. pH 7.8 V beta mercaptoethanol (DME)
Match the method for three-dimensional structure determination from the drop down menu to a property of the method. The macromolecules are in a packed, ordered array, yet still surrounded by water. Multiple pictures from different points of view are combined. 1. X-ray crystallography Samples are flash frozen. 2. Nuclear magnetic resonance 3. Cryoelectron microscopy Multiple conformations are superimposed to show the range of motion of the molecule. v A two-dimensional version of method gives atom to atom distances
The principal determinant of the fold a protein takes is A/ The other factor is A/ , especially A . The effect in blank 2 can be negative, leading to A Chaperone proteins prevent this by isolating the protein from the (repeat blank 2) A in Word well: a folding chamber covalent crosslinking its amino acid sequence its environment misfolding other proteins the endoplasmic reticulum the Golgi complex the ribosome the mRNA the DNA gene control elements unfolding