The full amino acid sequence of FABP6 isMAFTGKFEMECEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKECNIQTMGGKTFKATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKRLAFor the next step in your analysis, you ran a BLAST search of the PDB of this sequence and found a structure that is 59% identical to thesequence of your protein. The following is the alignment of two sequences (with your protein in blue (FABP6) and the homologous structure inred (3ELX)):Expect score = : 4 × 10−4² and Identities = 69/116(50%), Positives = 88/116(75%)3ELX: 5 AFNGKWETECQEGYEPFCKLIGIPDDVIAKGRDFKLVTEIVQNGDDFTWTQYYPNNHVMT 64AF GK + E EC++ Y+ F KL GI DVI K R+FK+VTE+ Q+G DFTW+Q+YFABP6: 2 AFTGKFEMECEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMT 613ELX: 65 NKF IVGKECDMETVGGKKFKG IVSMEGGKLT IS FPKYQQTTEISGGKLVETSTASG 120NKF VGKEC+++T+GGK FK V MEGGKL ++FP Y QT+EI G KLVE ST GFABP6: 62 NKFTVGKECNIQTMGGKTFKATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGH MT117The identical amino acids are shown in black between the two sequences. A notation of "+" indicates a similar, but not the same, amino acid.The sequences are arranged to show overlap and gaps in the primary amino acid sequence. Part F - Identifying conserved residues from the BLAST alignmentIf an amino acid is found at the exact same location in the alignment of two homologous proteins, that amino acid is said to be "absolutelyconserved." An amino acid type can also be conserved at a given position. Using the BLAST sequence alignment above, sort alignedresidues into the appropriate categories.Drag the appropriate alignments to their respective bins.► View Available Hint(s)I→LQEV→QD→SAbsolutely conservedW→FT→MD→NConserved by typeN→GK→KA→ENot conservedReset Help

We know that proteins are made up of different amino acids. 2 amino acids differ from each other…

Answered: Part F - Identifying conserved residues…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 20P

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Similar questions

Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?
Provide the number of polypeptide chains present andthe number of amino acid residues in each chain. for https://www.rcsb.org/structure/6j20 Provide the molecular weight of the protein orprotein complex and the total number of atoms. (All of this information can be found in the PDBpage.) Create a figure (available in the PDB page) that shows the topology of your protein, i.e.the secondary structures adopted by different regions of the protein (alpha helix, beta strand).Make sure to also provide a figure legend that helps interpret the figure and appropriate figurecaption that briefly explains the figure.
A protein hypothetically consists of two polypeptide chains with the given sequences in the picture. Based on the said sequences, a. Do you think it is possible that interchain disulfide bonds is present in the protein? Explain. b. Do you think it is possible that intrachain disulfide bonds is present in the protein? Explain.
Protein-4YU4 is given, choose a part of it (containing at least 30 amino acid residues), find the amino acid sequence (sequence in it), identify what functional groups the amino acid substitutes contain (carboxyl group and 2-position the Nitro group will form amide bonds, forming the covalent basic structure of the protein). What different interactions can occur between these functional groups? How will it relate to the spatial structure of the protein?
A protein is found to be a tetramer of identical subunits. Name two symmetries possible for such a molecule. What kinds of interactions (isologous or heterologous) would stabilize each?(a) Suppose a tetramer, like hemoglobin, consists of two each of two typesof subunits, α and β. What is the highest symmetry now possible?
The following are sequences from three different alpha helices found inhuman proteins: hBak(72-87): GQVGRQLAIIGDDINR hCB1(196-210): VTASFTASVGSLFLT hCB2(248-262): LVLAVLLICWFPVL Classify each of these three helices as either a) mostly hydrophobic, b)mostly hydrophilic, or c) amphipathic. Use the helical wheel to explainyour answers. Given the character of these helices, in which part of the protein wouldyou expect them to reside?
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 kDa
A molecule of composition5′-AAAAAAAAAAA-3′3′-TTTTTTTTTTTTT-5′is replicated in a solution containing unlabeled (notradioactive) GTP, CTP, and TTP plus adenine nucleoside triphosphate with all its phosphorus atoms in theform of the radioactive isotope 32P. Will both daughtermolecules be radioactive? Explain. Then repeat thequestion for the molecule5′-ATATATATATATAT-3′3′-TATATATATATATA-5′
Common proteins are polymers of 20 different amino acids. How big a protein (how many amino acid residues) would be necessary to have an Avogadro’s number of possible sequences?
GT 3 A. Write the structure of the pentapeptide GLDSC. B. What is the complete name of this pentapeptide? Show a tertiary structure of ACGGC after a disulfide bond forms. A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin; the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C- terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn-Thr-Trp-Met-lle-Lys Gly-Tyr-Met-Gln-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen bromide treatment Gln-Phe Val-Leu-Gly-Met lle-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-Met
GTTTTCACTGGCGAGCGTCATCTTCCTACT 10. Generate a secondary structure prediction for one identified protein.
A fragment of a protein commonly found in food was sequenced and found to have the sequence: RDCEHKY Draw the structure, showing the form expected to be dominant at a physiological pH (7.4). Discuss how changing the pH will affect the fragment, and what implications this has on the overall structure of the protein. What is the difference between the sequence above and the sequence YKHECDR?

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