The following data describe the catalysis of cleavage of peptide bonds in small peptides by aprotease:Substrate K (1/s) K₁, (mM) k./K₁ (mM/s)A0.110B11100.11000.028,0000.0510,0000.5Use this information to answer the next three questions.BODEFсDEF0.0111005,000160,00020,0004. Which substrate binds to the enzyme with the highest affinity?a. Ab. BC. Cd. De. Ef. F

Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Answered: The following data describe the…

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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on -f ion Substituting antisense oligonucleotide non-bridging oxygen atoms with a sulpha atom: Select one: O a. Decreases oligonucleotide stability in biological fluids O b. Increases oligonucleotide hydrophobicity increasing the likelihood of it partitioning a O c. None of these Od. Increases oligonucleotide stability in biological fluids Oe. Has no effect on oligonucleotide stability in biological fluids Therapeutic replacement genes need to be delivered to which intracellular compartment? Select one: O a. The chloroplast O b. The lysosome The Nucleus O c. O d. The ribosome O e. The Golgi Give both answer only with little bit explanation Asap Thanks
Which of these amino acids is a polar, uncharged amino acid? (Select all that apply, if necessary.) A. B. D. E. CHLO H₂N-CH-C CH₂ CH₂ CH₂ NH C=NH2 NH₂ amino acid A amino acid C amino acid D amino acid B amino acid E H₂N-CH-C CH₂ _i_g C. H₂N-CH-C- CH2₂ I CH₂ =0 NH₂ H₂N-CH- CH₂ CH-CH3 CH3 H₂ND H₂N-CH- | CH₂ Ï OH
According to these data: Protein MW A. 125 43 55 C-7/D-48 C-7.0/D-7.5 92 3.9 C/D 11 F 14 6.5 C/D is a dimer What is the order of elution of a gel filtration column at pH= 8? Oal F. B. C/D, E, A OCFB. D. E. A OOAED, B. F. c OGAEC/D, B, F
Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala
Discuss the mechanism that leads to aggregation of a protein therapeutic via a conformationally-altered monomer. Suggest one method of minimising aggregation via the mechanism above. please only answer if you are goin to explain well
Identify which of the following pairs of amino acid residues can have hydrogen bonding between their side chains.a. Alanine and Glycineb. Leucine and Isoleucinec. Valine and Asparagined. Threonine and Tyrosine2. Draw a picture showing the details of the hydrogen bonding among the pairs in exercise 1
The transpeptidase activity of penicillin binding proteins (PBP) promotes: please explain and choice the roght answer a.the addition of N-acetyl glucosamine to N-acetyl muramic acid b.,peptide crosslink formation between murein subunits c.the addition of murein precursors to a growing polymer d.beta lactamase binding to PBP
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
Answer the following using the picture attached: A. How does pepsin differ from chymotrypsin in terms of its active site residues and mechanism? B. How do these changes permit pepsin to operate at such a low pH?
Identify which of the following amino acid residues can have hydrogen bonding between their side chain and the protein backbone. a. Tyrosine b. Alanine C. Leucine d. Asparagine Draw a picture showing the details of the hydrogen bonding between the side chain and the protein backbone for any amino acid residues from exercise 4 that are capable.
Indicate which of the following descriptions is true about the biochemical depicted here: NH₂ +41 5 HO- он он OH OH OH a. Ribonucleotide b. Complementary to dTTP c. Purine d. Key reagent in Sanger sequencing e. Answers b., c. and d. are correct
What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed values

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