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

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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?
Low-resolution X-ray diffraction analysis of a protein composed of long stretches of the sequence (-Gly-Ser-Gly-Ala-Gly-Ala-)n, where n indicates any number of repeats, shows an extended structure of stacked layers, with a repeat distance between layers that alternates between 3.5 Å and 5.7 Å. Propose a mođel that explains this scenario. 5. The right-hand panel in the linked figure shows sedimentation equilibrium analytical ultracentrifugation data for a mixture containing equimolar amounts of two fibrous proteins, Vps27 and Hsel. The blue circles are the data and the black line is the expected plot for a monodisperse 1:1 Vps27:Hsel complex of 23.7 kDa. In the left-hand panel, data is shown for Vps27 alone. The black line represents the expected curve for monomeric Vps27. Both experiments were run under identical conditions (same buffer, same spinning speed etc.) and the proteins have the same partial specific volume.
Purification of a protein of unknown structure has been achieved. The natural protein has a molecular weight of 240,000, according to size-exclusion chromatography. Using a concentration of 6 M guanidine hydrochloride in the chromatography, a single peak can be identified as the molecular weight (MW) 60,000 of a protein. B-mercaptoethanol (BME) and guanidine hydrochloride (GHC) are used in tandem to produce proteins with mass masses of 34,000 and 26,000, respectively. The structure of this protein can be inferred from these facts.
Marker Proteins Molecular Weight (daltons) Distance 132,000 66,000 43,000 14,400 Serum Albumin (Dimer) Serum Albumin (Monomer) 23mm 32mm Ovalbumin 39mm 60mm Lysozyme Unknown 1 26mm Unknown 2 58mm Rabbit serum (albumin) 33mm 1.On semilog paper (provided below) plot the distance migrated by each standard protein as a function of molecular weight. Determine the molecular weight of the unknown proteins and the major protein found in rabbit serum (albumin) from this calibration curve. ii) Interferon is a protein of 25,000 Dalton. How far would it have migrated, land it been included in this experiment? iii) The average amino acid residue in a protein has a molecular weight of 120 Daltons. Assuming that your unknowns are average, how many amino acid residues do they contain
DO NOT COPY OLDER ANSWERS! AND SHOW FULL WORK! I have a mixture of 4 proteins, whose sequences are shown below (note that each protein is a 100-repeat of the sequence shown). Protein A: (Gly-Ala-Lys-Val-Ile-Phe-Glu-Val-Asn-Gly) Protein B: (Ala-Ala-Lys-Arg-Ile-His-Glu-Ala-Asn-Lys) Protein C: (Glu-Val-His-Asp-Ala-Asp-Glu-Val-Asn-Asp) Protein D: (Ala-Lys-Arg-Phe-Trp-Phe-Gly-Ile-Ala-Gly) 1) Which protein/s are MOST LIKELY to precipitate out at a pH of 3.5? a) A b) B c) C d) D e) B & C f) A & D g) None of them h) Cannot be determined.
Approximate molecular weight for an unknown protein from gel-filtration experiment is 130 kDa. Thirty six mg of this pure protein was treated with excess of fluorodinitrobenzene. After the reaction and complete acid hydrolysis the mixture was found to contain 356 µg of dinitrobenzene derivative of methionine (free acid) and no other amino acid-dinitrobenzene derivatives. Is this protein consisting of single polypeptide chain or multiple subunits? If it consists of multiple subunits, then how many? From these data, can you calculate the molecular weight of the protein more precisely?
Affinity chromatography You have created a fusion protein tagged with Glutathione-S-Transferase (GST). Your lab mate tells you that the affinity columns for this type of tagged protein are very similar to that of Histadine tagged proteins. Using the following elements set up a purification column and construct a protocol for an affinity purification using this tag. A large amount of glutathione is usually used to elute the tagged protein off the column. How might this work?
Sequence: CCACCTGTACCCGGACACACCCTGGTGTCC What human disease has been connected to this gene? Calculate molecular weight (kiloDalton, kD) and calculated pI (the pH where the protein carries no net electrical charge) of the protein.
TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)
Help me
The peptide below -NH-CH- H3N-CH- CH3 NH-CH- -NH-CH- -O- -NH-ÇH- CH2 CH2 CH2 HN-ç=NH, NH2 CH2 CH2 CH Ho-CH, C-OH H,C CH3 needs to be separated from a second peptide with a primary sequence ADES. At what pH range would it be possible to separate the peptides? O 0- 2.0 O 2.5 - 3.5 O 4.0 - 9.0 O 13.0 -14.0 о 10.0-12.0
Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. What is the molecular basis for the differences in the electrophoretic mobilities of the four proteins analyzed in this exercises? size shape charge all of them

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