ill in the blank The portion of a polypeptide sequence that can fold and has its own particular function is called a ( ).
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The portion of a polypeptide sequence that can fold and has its own particular function is called a ( ).
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- A polyhistidine-tag or better known by its trademarked name His-tag is an amino acid motif present in the N or C terminus of proteins (recombinant) consisting of at least six histidine residues. Explain the importance of His-tag in protein work.Fluorescent proteins like the green fluorescent protein (GFP) found in jellyfish are a class of colorful proteins that shine a particular color when exposed to ultraviolet light. These proteins, despite exhibiting a wide range of diverse colors, have nearly identical secondary structure across organisms and phenotypes. Each GFP-like protein has a few alpha-helices as well as a characteristic beta-barre composed of 11 beta-sheets that shields the inside of the protein from solvent (i.e., water). The GFP like protein shown below is a green fluorescent protein from the great star coral Montastraea cavernosa and contains two alpha-helices in its structure (labeled A and B and colored cyan). A 1. Helix A contains 6 amino acids, including a phenylalanine and an aspartic acid. Which position (1 or 2, colored in red) would you more likely expect aspartic acid to be located? [ Select ] 2. If you were to compare helix A to helix B, would you expect the ratio of polar:non-polar residues to be…Using a copy of a helical wheel (attached to the end) plot the amino acids of the helix on the helical wheel. Is there any evidence of the helix as a whole being amphipathic or having a “sidedness"? Explain yes or no. Are the amino acid side chains in close proximity of one another or staggered to minimize steric hinderance between side chains? Explain the pattern you observe.
- Within a protein, certain amino acids are positively charged (e.g.,lysine and arginine), some are negatively charged (e.g., glutamateand aspartate), some are polar but uncharged, and some are nonpolar.If you knew that a DNA-binding protein was recognizingthe DNA backbone rather than a base sequence, which aminoacids in the protein would be good candidates for interacting withthe DNA?The variable structures of a nucleotide are the sugar and the phosphate group. (a). Say if the statement written above is true or false. (b). Give ONE reason for your answer in part (a).Draw a ribbon structure for the following polypeptide. There’s more than one answer to this question, make sure you are able to support your answer. Don’t have to write out the amino acids, just draw a line or ribbon, should include some numbers to indicate specific amino acids that you think will interact.
- It is often the case that a helices are positioned in a protein such that one side faces the interior of the protein and the other, the surface of the protein. These are said to be amphiphilic helices because they face different environments. Using a helical wheel projection (shown below), which of the peptide(s) below might form an amphiphilic helix? 8 15 1 12 4 11 16 18 9 7 14 13 10 17 O SLIKSVIEMVDEWFRTFL O FLIRVLRKVFRVLTRILS O RLFRSRVLKIAVIRFLLIFluorescent proteins like the green fluorescent protein (GFP) found in jellyfish are a class of colorful proteins that shine a particular color when exposed to ultraviolet light. These proteins, despite exhibiting a wide range of diverse colors, have nearly identical secondary structure across organisms and phenotypes. Each GFP-like protein has a few alpha-helices as well as a characteristic beta-barrel composed of 11 beta-sheets that shields the inside of the protein from solvent (i.e., water). The GFP- like protein shown below is a green fluorescent protein from the great star coral Montastraea cavernosa and contains two alpha-helices in its structure (labeled A and B and colored cyan). A B 1. Helix A contains 6 amino acids, including a phenylalanine and an aspartic acid. Which position (1 or 2, colored in red) would you more likely expect aspartic acid to be located? [Select] 2. If you were to compare helix A to helix B, would you expect the ratio of polar:non-polar residues to be…You are studying the toxic protein called ectatomin, a major component of ant venom (specifically from the species Ectatomma tuberculatum), that embeds into cell membranes and creates pores that cause cells to lyse. Ectatomin is a small dimer, meaning the protein is comprised of two polypeptides; the sequences of the two polypeptides are given in the table with single-letter abbreviations. polypeptide sequences of ectatomin monomers polypeptide protein sequence polypeptide 1 GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL polypeptide 2 WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK You could use absorbance at 280?? or colorimetric assays like the Bradford assay or bicinchoninic acid assay (BCA) assay to quantify the amount of ectatomin you have for your experiment. Why might you choose to use a colorimetric method instead of absorbance at 280??? Select the best answer. Measuring absorbance at higher wavelengths, like 595?? or 562??, is more accurate than measuring absorbance at…
- Name another condition besides heat and exposure to a bond disruptor (like alcohol) that could affect the ability of a protein to maintain its shape.Avidin exists as a protein complex of around 68 kDa. Research to determine the types of interactions that hold the avidin complex together. Based on your research, which molecular weight would you expect for avidin when treated with beta-mercaptoethanol and run through a native gel? 35 kDa 68 kDa 10 kDa 19 kDaIn the following polypeptide, which amino acid would be participating in hydrogen bonding with alanine, given this sequence forms an alpha helix? Please write out the full amino acid name, not the abbreviation. Met-Ala-Leu-Glu-Lys-Thr-Leu-Val