This image is showing the conformations of ubiquitin superimposed. What do the structures in this figure tell us about the dynamics of enzymes? Discuss the limitations of crystal structures in the analysis of proteins. What are the benefits? What are the advantages of NMR structures?

A) Identify the structures that would be found in proteins B) identify the structures that polymerize via condensation reactions

During successful purification of every enzyme, the following may be expected: Select ALL that apply. 1. Solubility in NaCl increases 2. The activity increases 3. The specificity increases 4. The number of subunits increases 5. the epitope number increases

There are 4 classes of biochemical families (Carbohydrates, Proteins, Lipids, and Nucleic Acids). Identify the biochemical family that is described by the statements below. 1. The monomer of this biochemical family is called an amino acid. 2. DNA is an example of this biochemical family. 3. Glucose and sucrose are an example of this biochemical family. 4. Vitamin A, steroids, waxes, and phospholipids are all examples of this biochemical family. 5. This diverse biochemical family is known for being nonpolar and insoluble in water. 6. This biochemical family is the genetic material in an organism and is made up of a phosphate, sugar, and base monomer. 7. The monomer of this biochemical family contains an amine and a carboxylic acid functional group. Two monomers are linked together through condensation polymerization of these two functional groups.

A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown here. Only one of the Cys has a free —SH group, and the other two are involved in an —S—S— bond. The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., withdisulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the —S—S— bond (i.e., AB, BC, or AC)?

Imagine that you were asked to denature a protein; you know you can do so using urea.  Your protein binds ATP (a nucleotide). You decide to add ATP to your denatured protein:urea mixture and then add water to dilute the urea and facilitate refolding of the protein.  How do you expect the addition of the ATP will affect the free energy of refolding?  Consider Gibbs free energy.

Can I get a visual (drawn on paper or on a software; like chem draw or chem sketch)? Illustrate detailed chemical scheme for how you will functionalize your biomolecule to the surface of the sensor (e.g. if you wanted to functionalize a protein to a gold SPR chip, you should could show the assembly of an amine-terminated SAM, followed by carbodiimide coupling of. the protein). These schemes should be drawn using a chemical illustration software package (ChemDraw / ChemSketch).Your chemical schemes should be as detailed as necessary to accurately depict the chemical design of your system, DO NOT INCLUDE a step-wise mechanism, it is not necessary. You should include at least one literature reference to support your conjugation strategy.

The E. coli enzyme triose phosphate isomerase has a pI of 5.7. What would the charge on this enzyme be below a pH of 5.7? What about above? What would the charge be at a pH of 5.7?

detail how cation exchange chromatography works and what you would use to elute your target protein. What protein information would you need to facilitate this approach? Would you need to do any protein engineering to utilize cation exchange chromatography, justify your answer?

What happens when an enzyme is denatured? Can a denatured enzyme be "re-natured"? Explain.