2. The mature form of TEM-1 ß-lactamase, an enzyme of 290 amino acid residues that hydrolyzespenicillin antibiotics. The protein has the following polar amino acid side chains: 18 Arg; 11 Lys; 6 His;4 Tyr; 16 Asp; 20 Glu; 8 Asn; 5 Gln.Approximate pKa values1.5Arginine12.5Lysine10.0Histidine6.5OD280nmTyrosine10.0Aspartate orGlutamate4.0Terminal NH3+8.0Terminal COOH4.00.0A0.01 0.10 KCIBVolume (mL)The chromatogram above shows a typical result in the purification of TEM-1 ß-lactamase overex-pressed in E. coli cells. The protein is eluted from an anion exchange column at pH 6.25 with an increasinggradient of KCI. Fraction A is shown to correspond to native enzyme. Since Fraction B has the same amino acidsequence for the first 10 residues, the conclusion is that this fraction represents enzyme in which sidechains of glutamine or asparagine residues have been hydrolyzed (deamidated).(a) () What is the isoelectric point of the native enzyme?(b) () Compared to the native protein, in which direction will the isoelectric point of the deamidatedprotein change? How will the change in isoelectric point affect the overall charge on the protein at pH6.25?

Before calculating the isoelectric point (pI) of the enzyme, we need to be thorough with the…

Answered: 2. The mature form of TEM-1…

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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Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the cDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide Hexanucleotide Nonanucleotide Decanucleotide Dodenucleotide Octadecanucleotide Nonadecanucleotide 21-nucleotide The mutation involved the 19th bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptide (N) and mutant peptide (M) is shown below. The (+) electrode is situated at the bottom. pH…
What is the role of his 12 in the RNase-catalyzed hydrolysis of RNA, as indicated in the Figure below? 5' His 119 RNA CH₂ H H 3 O Base 1' 12' 8-H His 12 -P-0-CH₂ a Base H H O -0-P=O H OH NH It acts as a general base, abstracting a proton from the 2' hydroxyl in order to increase its nucleophilicity. It forms an H-bond with his119 in order to stabilize the transition state. It donates a proton to improve the quality of the leaving group. It works through concerted general acid-base catalysis with his119 in order to favour the products of the reaction. Two of the above are true.
Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.
I'm conducting an experiment concerned with the binding affinity of tretinoin (all trans retinoic acid) and beta lactoglobulin. This can be accomplished by monitorization of fluorescence quenching of a tryptophanyl residue that resides in a hydrophobic pocket known as a calyx inside the protein. Generally, fluorescence quenching is classified as static or dynamic. Would fluorescence quenching be a result of amide bond formation to tryptophan from tretinoin or through another mechanism (ie FRET: Forester resonance energy transfer)? Could it be both?
A peptide with endorphin-like property was produced and obtained from the blood. This was sequence using the protocol: Treatment with streptococcal protease gave a tripeptide and a tetrapeptide. Treatment with trypsin gave two tripeptides and an amino acid. Treatment of the 2 tripeptide products in 1.2 with 2,4-dinitrophenol gave DNP- S, and DNP-E and a mixture of amino acids. The composition of the peptide is G, E, S, and K in a 2:1:1:3 molar ratio. a. Determine the sequence of the peptide? b. Determine the pl and position in an electrophoretic profile
You are presented with Cytidine 5' triphosphate and Thymidine 5' triphosphate. Draw and upload to Efundi these phosphorylated structures as they would be connected in a polinucleotide in the order CpT / Show the individual phosphorylated structures first then show how they combine to form the polynuleotide. Show at any one of these structures where the glycosidic bond occurs
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
Liposomes used in these vaccines contain some cationic lipids, or lipids with a positively charged head group. Explain why this is a sensible strategy for delivering genetic materials (or drugs) to a human cell.
10
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A researcher has synthesized two peptides and needs to confirm whether the peptides were synthesized with the correct sequence using mass spectrometry. What is the sequence of the b4 and y7 ions for peptide GAMECHANGER? The peptide SLISRAEFLAGVRVGV is digested with trypsin. Then the products of the digestion are subjected to ESI TOF-MS in positive ion mode with the peptides in a pH 2 solution. What peptide fragments will result and what are their m/z?
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