CONNECT IA GENERAL ORGANIC&BIO CHEMISTRY
4th Edition
ISBN: 9781260562620
Author: SMITH
Publisher: MCG
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Chapter 21.10, Problem 21.14P
Interpretation Introduction
Interpretation:
The optimum pH from the graph needs to be estimated for the hydrolysis of proteins in small intestine by trypsin enzyme.
Concept introduction:
Enzymes are proteins that help in fastening the
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Chapter 21 Solutions
CONNECT IA GENERAL ORGANIC&BIO CHEMISTRY
Ch. 21.2 - In addition to the amino and carboxyl groups, what...Ch. 21.2 - Draw both enantiomers of each amino acid in...Ch. 21.2 - Which of the following amino acids is naturally...Ch. 21.3 - Draw the structure of the amino acid valine at...Ch. 21.3 - Identify the amino acid shown with all uncharged...Ch. 21.4 - Identify the N-terminal and C-terminal amino acid...Ch. 21.4 - Prob. 21.4PCh. 21.4 - Prob. 21.4PPCh. 21.4 - Prob. 21.5PCh. 21.4 - Prob. 21.5PP
Ch. 21.4 - Prob. 21.6PPCh. 21.5 - Prob. 21.6PCh. 21.6 - Prob. 21.7PCh. 21.6 - Prob. 21.8PCh. 21.6 - Prob. 21.9PCh. 21.7 - Why is hemoglobin more water soluble than ...Ch. 21.8 - Prob. 21.7PPCh. 21.8 - Prob. 21.11PCh. 21.9 - Prob. 21.8PPCh. 21.9 - Prob. 21.12PCh. 21.9 - Prob. 21.9PPCh. 21.9 - Prob. 21.13PCh. 21.10 - Prob. 21.14PCh. 21.10 - Prob. 21.15PCh. 21.10 - Prob. 21.16PCh. 21.10 - Prob. 21.17PCh. 21.10 - The nerve gas sarin acts as a poison by covalently...Ch. 21.10 - Prob. 21.19PCh. 21.10 - Explain why the proteins involved in blood...Ch. 21 - The amino acid alanine is a solid at room...Ch. 21 - Why is phenylalanine water soluble but...Ch. 21 - Draw the structure of a naturally occurring amino...Ch. 21 - Draw the structure of a naturally occurring amino...Ch. 21 - For each amino acid: [1] draw the L enantiomer in...Ch. 21 - For each amino acid: [1] draw the L enantiomer in...Ch. 21 - Draw both enantiomers of each amino acid and label...Ch. 21 - Which of the following Fischer projections...Ch. 21 - For each amino acid: [1] give the name; [2] give...Ch. 21 - For each amino acid: [1] give the name; [2] give...Ch. 21 - (a) Identify the amino acid shown with all...Ch. 21 - Prob. 32PCh. 21 - Prob. 33PCh. 21 - Draw the structure of the neutral, positively...Ch. 21 - Locate the peptide bond in the dipeptide shown in...Ch. 21 - Label the N-terminal and C-terminal amino acids in...Ch. 21 - Melittin, the principal toxin of bee venom,...Ch. 21 - Cobratoxin is a neurotoxin found in the venom of...Ch. 21 - (a) Draw the structure of the two possible...Ch. 21 - (a) Draw the structure of the two possible...Ch. 21 - For each tripeptide: [1] draw the structure of the...Ch. 21 - For each tripeptide: [1] draw the structure of the...Ch. 21 - Prob. 43PCh. 21 - For each tripeptide: [1] identify the amino acids...Ch. 21 - What amino acids are formed by hydrolysis of the...Ch. 21 - Prob. 46PCh. 21 - Prob. 47PCh. 21 - Draw the structures of the amino acids formed when...Ch. 21 - Prob. 49PCh. 21 - Prob. 50PCh. 21 - Prob. 51PCh. 21 - Trypsin is a digestive enzyme that hydrolyzes...Ch. 21 - What type of intermolecular forces exist between...Ch. 21 - What type of interaction occur at each of the...Ch. 21 - Which peptide in each pair contains amino acids...Ch. 21 - Decide if the side chains of the amino acid...Ch. 21 - Which type of protein structure is indicated in...Ch. 21 - Label each of the following diagrams as...Ch. 21 - Prob. 59PCh. 21 - Prob. 60PCh. 21 - Prob. 61PCh. 21 - Prob. 62PCh. 21 - Compare - keratin and hemoglobin with regard to...Ch. 21 - Compare collagen and myoglobin with regard to each...Ch. 21 - Prob. 65PCh. 21 - Prob. 66PCh. 21 - Describe the function or biological activity of...Ch. 21 - Describe the function or biological activity of...Ch. 21 - Prob. 69PCh. 21 - Prob. 70PCh. 21 - What class of enzyme catalyzes each of the...Ch. 21 - What class of enzyme catalyzes each of the...Ch. 21 - Prob. 73PCh. 21 - Prob. 74PCh. 21 - Prob. 75PCh. 21 - What kind of reaction is catalyzed by each of the...Ch. 21 - Prob. 77PCh. 21 - How will each of the following changes affect the...Ch. 21 - Prob. 79PCh. 21 - Prob. 80PCh. 21 - Prob. 81PCh. 21 - Prob. 82PCh. 21 - Prob. 83PCh. 21 - Prob. 84PCh. 21 - Prob. 85PCh. 21 - Prob. 86PCh. 21 - Why must vegetarian diets be carefully balanced?Ch. 21 - Prob. 88PCh. 21 - Sometimes an incision is cauterized (burned) to...Ch. 21 - Why is insulin administered by injection instead...Ch. 21 - Prob. 91PCh. 21 - The silk produced by a silkworm is a protein with...Ch. 21 - Explain the difference in the mechanism of action...Ch. 21 - Prob. 94PCh. 21 - Prob. 95CPCh. 21 - Suggest a reason for the following observation....
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- The pH at which the concentration of the zwitterionic form (dipolar form) of an amino acid is at its highest and the concentrations of the cationic and anionic forms are equal is called the ___.arrow_forwardConsider an amino acid with the following pKa values: pKa1 = 2.71 and pKa2 = 9.31 At what pH value in aqueous solution would this amino acid (its predominant form) exist as an anion?arrow_forwardDraw the sequential transition of glutamic acid as it passes from its fully protonated form to its fully deprotonated form as the pH rises. If the pH of an amino acid solution is lowered by adding an acid, like , the group of glutamic acid accepts the proton, acid, to form a positive ion.arrow_forward
- The side chain of cysteine is weakly acidic. Suppose in a protein, the side chain of a cysteine residue is surrounded by the side chains of several isoleucine residues. Would this make the side chain of the cysteine residue more acidic or less acidic? Please explain your answer.arrow_forwardExplain which amino acids are acidic, which are basic, and which are neutral. Use theisoelectric point to predict whether a given amino acid will be positively charged,negatively charged, or neutral at a given pH.arrow_forwardWould alpha-D-glucopyranose and alpha-D-fructopyranose be equally likely to be the substrate for a given enzyme? Refer to both shape and noncovalent interactions in your answer. Make one generalization about protein-carbohydrate interactionsarrow_forward
- Answer the following questions on the basis of the free energies of formation at 25°C shown in the table at the top of the next page: (a) Does the peptide bond between alanine and glycine form spontaneously under standard conditions?arrow_forward. Describe the pH range of acceptable buffering behavior for the amino acids alanine, histidine, aspartic acid, and lysine.arrow_forwardOxygen is transported around the body by the globular protein hemoglobin which contains four Fe2* ions. Hemoglobin is “oxygenated" when coordinated to dissolved oxygen in the blood. This can be simplistically represented by the following equation (where Hb represents one hemoglobin molecule): н (ад) + 402 (д) + нь(02)4 (аq) (1) Hemoglobin also readily binds with carbon monoxide (CO). Indeed, hemoglobin has a much higher affinity to CO than O2 resulting in significantly stronger hemoglobin binding to CO than to O2. This is a problem because hemoglobin molecules which are coordinated to carbon monoxide are unable to transport oxygen around the body as needed. No more than 2.5% of your body's hemoglobin can be bound to CO before health effects become noticeable. The consequence is that even very low partial pressures of CO in the air have physiological implications for humans. нь (ад) + 4Cо (д) + нь(со)4 (аq) (2) Compare and evaluate the relative magnitudes of the equilibrium constant for…arrow_forward
- You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows:Histidine 7.64Lysine 9.74Cystenie 5.02Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixturearrow_forwardAll amino acids have two ionizable functional groups: an a-amino group (average pK, of 9.4) and an a-carboxylic acid group (average pK, of 2.2). Glutamic acid has an ionizable side chain (R group) with a pK, of about 4.1. One of the possible ionization states of glutamic acid is shown in the image. H₂N-CH-C-OH CH₂ At what pH would this structure of glutamic acid be the predominant ionization state? Consider the ionization state of all three of the functional groups. OH The protonated form of the R group of glutamic acid is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the pK, of the R group and the pH of the solution. 2.6 4.1 1.5 Select the pH values at which the charged form of the R group would predominate. 7.0 11.3arrow_forwardThe first step in the procedure asks you to prepare five dilutions of the protein standard (BSA) in the range of 0.2 to 1.0 mg/ml. For each concentration, a volume of 1.0 mL should be prepared. Describe how you will prepare these standards using a stock solution of BSA that is 2.0 mg/ml.arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY