Decide whether each of the following statements is true about ornithine carbamoyltransferase. It's a small molecule, with a molecular weight around 50 mol It's made by a ribosome out of amino acids. It's a substrate, and ornithine is its superstrate. It has no effect on the stability of ornithine, that is, it does not change the free energy of ornithine. O true false true false Otrue false O true false

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?

Please help me with this question.   How many amino acid residues are in the heavy and light chains of the Fab fragment, and how many amino acid residues are in lysozyme?

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what is lactose intolerance ? describe the molecular life cycle for this disease. also describe how it occurs in a molecular level detailed mechanism. what causes this disease and how it develops ? provide detailed biochemical phenomena and life cycle for Lactose Intolerance condition.

Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent?  Your reply will be greatly appreciated.  The ligand that was assigned to me is tadalafil.

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Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme                Km (M)                       kcat (1/s)Chymotrypsin       1.5 × 10^−2                   0.14Pepsin                   3.0 × 10^−4                   0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4        7.6Ribonuclease        7.9 × 10^−3               7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2             4.0 × 10^5Fumarase               5.0 × 10^−6                  8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?

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The allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!