1. You are studying an E. coli gene that specifies a protein. A part of its sequence is -Ala-Pro-Trp-Ser-Glu-Lys-Cys-His You recover two mutants for this gene that show no enzymatic activity. By isolating the mutant enzyme products, you find the following sequences: Mutant 1: Ala-Pro-Trp-Arg-Glu-Lys-Cys-His Mutant 2: Ala-Pro- What is the molecular basis for mutation 1 and for mutation 2? What is the DNA sequence that specifies this part of the protein? Wild-type amino acid sequence: NH3-Ala-Pro-Trp-Ser-Glu-Lys-Cys-His-COOH Mutant 1: NH3-Ala-Pro-Trp-Arg-Glu-Lys-Cys-His-COOH Mutant 2: NH3-Ala-Pro-

4). Mutants unable to synthesize an essential compound G were tested with related compounds D, E, and F. The results are summarized below, where + indicates growth, and 0 indicates no growth. Mutants 1 2 3 4 D 0 0 0 Compounds E 0 INAAL F 0 0 INAY a). What is the order of gene action in the biosynthetic pathway? G

You have discovered a novel protein that has a pl = 5.5. To study the functional properties of this new protein your research group has made a mutant that contains two amino acid changes-namely, a surface Phe residue in the normal protein has been replace by His (side chain pk = 6.1), and a surface Gln has been replace by Glu (side chain pk. = 6.0). The pl of the mutant protein is predicted to be: A. Greater than the pl of the normal protein. B. Less than the pl of the normal protein. C. The same as the pl of the normal protein.

Once the chains of peptides that make up lysyl-tRNA synthetase protein are synthesized in ribosomes, lysyl-tRNA synthetase needs to have the proper active site in order to perform its function, explain the process of protein folding necessary to have a proper 3-D structure, include effect of thermodynamics and different states in folding, including what happen when there are prolines that form peptide bonds with other amino acids, and any disulfide bridges

13) A researcher is studying the synthesis of a specific amino acid found in Neurospora. She knows that the pathway begins with a precursor that is converted into the amino acid with two known intermediates (Substance Blue and Substance Green). She accurately predicts that this amino acid synthesis pathway is catalyzed by three enzymes, (I, II, and III). She subsequently identifies three mutants that she calls Mutant I, Mutant II, and Mutant III. With the information about the mutants 13) below place the enzymes in the order that the enzymes act in this pathway. (Note: the numbers I, II, don't necessarily indicate the order in which the enzymes appear.) Mutant I (only Enzyme I is mutated) is unable to synthesize the amino acid even if she provided the mutant with both Substance Blue and Substance Green. Mutant II (only Enzyme II is mutated) is able to synthesize the amino acid if she provided the mutar Substance Blue or Substance Green. Mutant III (only Enzyme III is mutated) is able…

If tRNALeu is mutated so that it is recognized by the tRNAVal synthetase but not the by tRNALeu synthetase, how will the following peptide sequence change upon mRNA translation? wild-type: Met-Lys-Leu-Pro-Ala-Leu-Val-Val-Ala O Met-Lys-Leu-Pro-Ala-Leu-Leu-Leu-Ala O Met-Lys-Val-Pro-Ala-Val-Leu-Leu-Ala O Met-Lys-Val-Pro-Ala-Val-Val-Val-Ala

1. What is the length in AA’s of the LilP protein? Assume fMet is NOT CLEAVED. 2. Write out the sequence of the polypeptide in AA: use the three letter notation, e.g. Met-Ser-Pro-

I'm a bit confused about this question  will someone help me understand the concept

How many Fnu4H1 sites do you find in this sequence? (in other words, how many times will this enzyme cut this sequence?) Reminder Fnu4H1 recognition site is:  5'-GC*NGC-3'3'-CGN*CG-5' The * indicates the cut site and N indicates any nucleotide

Please help with this as soon as you can, thank you.