This figure shows the results of a 2-dimensional gel that wa…

This figure shows the results of a 2-dimensional gel that was run to separate the proteins found in a snake toxin. Locate the prominent dark spot in the upper right-hand quadrant on the 2-dimension gel and answer these questions.  Name one thing that you can infer about that amino acid composition of this major spot from the isoelectric focusing direction of the gel?  What is one thing that you can infer from the PAGE direction of this gel about this protein? Image Source: Hatakeyama, et al. (2018) Image Description  A 2-Dimensional Electrophoresis (2-DE) gel showing the separation of proteins. The x-axis represents the pH range from 3 to 10, and the y-axis represents molecular weight from 15 kDa to 250 kDa. Multiple protein spots are visible, indicating their isoelectric points and molecular weights. The label “A” marks a significant area of interest on the gel. The gradient shading reflects the concentration of proteins, with darker spots representing higher protein abundance.

 The G-75 fraction that contains the desired biological acti…

 The G-75 fraction that contains the desired biological activity is further separated on a Mono-S column, which is a cation exchange column. Briefly describe the characteristics of a protein that binds to a Mono-S column and the role of the NaCl gradient in this type of chromatography.

  Upload an image of your answer to this question. Draw the…

  Upload an image of your answer to this question. Draw the complete structure of a tripeptide (three amino acid residues) of your choice that contains an amino acid with a neutral R group capable of forming H-bonds (residue 1), a second amino acid with an R group that has an isopropyl structure (residue 2), a third amino acid with an R group containing two fused aromatic rings (residue 3). Label each amino acid with its three-letter code and assume a pH of 7.4.  

Questions 2–9 refer to this toxic peptide. General Instructi…

Questions 2–9 refer to this toxic peptide. General Instructions: If the question does not require you to draw a structure, you may answer using either the full name of an amino acid or use its three-letter or single-letter code.   Many animal toxins are peptides. One of these is a 42-residue toxic peptide found in the South American rattlesnake, Crotalus durissus terrifics. The primary sequence of this peptide is shown below and its structure is shown in the figure. YKQCHKKGGHCFPKEKICLPPSSDFGKMDCRWRWKCCKKGSG Image Description  A 3D protein structure showing the positions of cysteine residues (Cys4, Cys11, Cys18, Cys30, Cys36, and Cys37) highlighted in yellow. The protein has an N-terminal (N) and C-terminal (C) with distinct secondary structures: alpha-helices in red and beta-sheets in blue, connected by green loops. The cysteine residues form disulfide bonds, contributing to the protein’s stability and shape.

Sephadex G-75 is a gel filtration or size exclusion solid ph…

Sephadex G-75 is a gel filtration or size exclusion solid phase chromatography material. It has it has a molecular weight cutoff range of >80 kD, where kD stands for kiloDalton (1 Dalton is 1 atomic mass unit). Briefly describe how this column functions and is able to separate a protein with a molecular weight of 100 kD from a protein with a molecular weight of 45 kD.

Isoelectric focusing gel electrophoresis separates non-denat…

Isoelectric focusing gel electrophoresis separates non-denatured proteins and peptides by their isoelectric points using a pH gradient gel. Would you predict that this peptide would stop its travel through the gel in the acidic or basic portion of the gel? Briefly justify your choice.