Refer to the given figure below. Peptide and protein synthesis in the bodyoccurs at the ribosome. In the molecular level, what happens is thereaction between the carboxyl moiety of one amino acid (BLUE), and theamino moiety of another amino acid (RED). What type of reaction occursin peptide synthesis?R1LOH + H2N.R2|- HOHR1H.R2O Unimolecular nucleophilic substitution (SN1)O Bimolecular nucleophilic substitution (SN2)O Nucleophilic acyl substitution (SNAC)O Unimolecular elimination (E1)O Nucleophilic addition (ANu)IZZIZI Refer to the given figure below. Peptide and protein synthesis in the bodyoccurs at the ribosome. In the molecular level, what happens is thereaction between the carboxyl moiety of one amino acid (BLUE), and theamino moiety of another amino acid (RED). What is the role of the redamino acid in the reaction?R1COH + H2N.H.R2|- HOHR1'N'H.Brønsted acidO Brønsted baseElectrophileO NucleophileO Radical

Elimination reactions are those in which a substance is eliminated during the course of the…

Refer to the given figure below. Peptide and protein synthesis in the body occurs at the ribosome. In the molecular level, what happens is the reaction between the carboxyl moiety of one amino acid (BLUE), and the amino moiety of another amino acid (RED). What type of reaction occurs in peptide synthesis? R1 of LOH + H2N. R2 - HOH R1 'N' R2 Unimolecular nucleophilic substitution (SN1) Bimolecular nucleophilic substitution (SN2) Nucleophilic acyl substitution (SNAC) Unimolecular elimination (E1) Nucleophilic addition (ANu) IZ ZI ZI

Refer to the given figure below. Peptide and protein synthesis in the body occurs at the ribosome. In the molecular level, what happens is the reaction between the carboxyl moiety of one amino acid (BLUE), and the amino moiety of another amino acid (RED). What type of reaction occurs in peptide synthesis? R1 of LOH + H2N. R2 - HOH R1 'N' R2 Unimolecular nucleophilic substitution (SN1) Bimolecular nucleophilic substitution (SN2) Nucleophilic acyl substitution (SNAC) Unimolecular elimination (E1) Nucleophilic addition (ANu) IZ ZI ZI

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

Protein denaturation can alter the 3 dimensional shape of a protein alter the sequence of amino acids in protein Obreak the peptide bonds holding the protein together Other: What is the purpose of using enzyme in detergent industry? all of the statements are true Enzymes are used to remove protein stains O Enzymes are used to remove human sweat which have a tendency to adhere strongly on textile fibers O Enzymes are used to improve texture of cloth or fiber Other: When an enzyme becomes saturated with its substrate, the rate of reaction vs concentration of enzyme graph line becomes a plateau. To produce a significant change in the reaction rate O the pH must be decreased O the temperature must be increased O the concentration of the enzyme must be increased O the pH must be increased
Following is the structure of a peptide with the name seryllysylaspartate. What is the amino acid at the N-terminus of this peptide? NH3 CH₂ 0 | CH₂ | CH₂ | CH, O || OH I CH, O || C | CH, O || H₂N-C-C-N-C-C-N-C-C-O I H | I | | HH HH O seryllysine O aspartate O lysine O serine 0=
Can I have a check on questions 5-8
Hi Need answers for the above question kindly help anyone.
The compound shown below is used to fluorescently label proteins: но. HO Which of the following statements about the reactivity of compound (1) with proteins is CORRECT? Compound (1) reacts with tyrosine residues in the protein to form a stable thiourea linkage. O Compound (I) reacts with tyrosine residues in the protein to form a stable amide linkage. O Compound (1) reacts with lysine residues in the protein to form a stable amide linkage. O Compound (I) reacts with lysine residues in the protein to form a stable thiourea linkage.
Looking at the protein structure below, what would be an accurate way to describe the circled portion? Prosthetic group binding motif a. Domain c. Tertiary structure d. Quaternary Structure Subunit Of. Primary Structure
Histones are proteins found in eukaryotic cell nuclei. They wrap DNA around itself, thereby compacting the phosphate-rich DNA the nuclei. Histones have a very high pI, usually around 10.8. What amino acid residues must exist in relatively large numbers in Histones? In what way do these residues contribute to the strong binding of Histones to DNA? Where do you expect the majority of these residues to be situated on the histone protein structure?
Considering the peptide structure on the image, label N-terminus and C-terminus, circle each of the peptide (amide) bonds, and provide the primary sequence of the protein using three letter abreviaciones for the amino acids
Chemistry Question
H₂N Combination of two or more protein units 7. Which type of cross-link involves interactions between two cysteine amino acids? 8. Which type of cross-link would form between the following amino acids? Η Ο || H₂N-C-C-OH T CH₂ C=O NH₂ Η Ο LL H₂N-C-C-OH T CH₂ OH 9. To what main enzyme class do the nzym that catalyze the following reaction belong? (oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) HO | || I c-c-N-C-COO + H₂O IT HR₂ R₁ H 1 This bond is cleaved H H₂N-C-COOⓇ I R₂ Wilter navy q H I H₂N-C-C00 1 R₁ •Qisulfide 10. Briefly explain the Lock and Key enzyme model.
How many peptide bonds in the following peptide are depicted as trans? H3C H. H нн N. 'N' H CH3 H CH2OH
3. what are the different test for carbohydrates, protein, lipids, and nucliec acid used to determine the presence of biomolecules? enumerate the indicators the used for each test.