Chemistry • Class 12
Biomolecules - Class 12
Master Biomolecules — Chemistry through focused practice that strengthens conceptual understanding, problem-solving skills, and the ability to recognize common traps and misconceptions. Explore challenging questions designed to develop deeper reasoning and confident application of key ideas.
Overview
This chapter covers carbohydrates, proteins, enzymes, lipids, nucleic acids, and vitamins. Learn about their classification, structure, and biological significance in living organisms.
Why This Chapter Matters
- Biomolecules are the building blocks of life. Understanding their chemistry is essential for fields like medicine, biotechnology, and nutrition science, making this chapter vital for advanced studies.
Real-Life Applications
- Understanding the role of biomolecules in cellular processes and metabolism.
- Exploring their applications in medicine, such as drug development and diagnostics.
- Analyzing the nutritional and biochemical roles of biomolecules in maintaining health.
Skills You Will Learn
- Classifying carbohydrates, proteins, lipids, and nucleic acids.
- Understanding the structure and function of enzymes and vitamins.
- Learning the biochemical significance of biomolecules in living systems.
Core Concepts to Master
D-Glucose Anomeric Equilibrium
Mutarotation involves interconversion via open-chain; equilibrium ratio is fixed (alpha 36%, beta 64%) in aqueous solution.
Epimerization vs Anomerization
Anomers differ at C1; Epimers differ at any other chiral center. Distinction is vital for nomenclature.
Glycosidic Linkage Geometry
Alpha-linkages (1->4) create helical structures (starch); Beta-linkages (1->4) create linear, rigid structures (cellulose).
Reducing Sugar Criteria
Must possess a free hemiacetal/hemiketal group. Check if the anomeric carbon is involved in the glycosidic bond.
Amino Acid Zwitterion pH Sensitivity
Isoelectric point (pI) calculation depends on pKa values of side chains; net charge changes with pH flux.
Protein Denaturation Specificity
Secondary/Tertiary structures break via H-bonding disruption, but primary peptide sequence remains intact during mild denaturation.
Osazone Formation Logic
Three equivalents of phenylhydrazine are needed; C1 and C2 configurations become identical, masking C2-epimer differences.
Nucleoside vs Nucleotide
Nucleotide contains a phosphate group attached to the 5' carbon of the sugar; nucleoside lacks phosphate.
Base Pairing Stability
G-C (3 H-bonds) is thermally more stable than A-T (2 H-bonds). Higher G-C content increases melting temperature.
Kiliani-Fischer Chain Extension
Cyanohydrin synthesis increases carbon chain length, creating two diastereomers differing at the newly formed chiral center.
Nitrogenous Base Keto-Enol Tautomerism
Tautomeric shifts lead to rare base-pairing mismatches, causing spontaneous point mutations in DNA replication.
Disaccharide Hydrolysis Products
Maltose (Glu+Glu), Lactose (Gal+Glu), Sucrose (Glu+Fru). Note sucrose is non-reducing due to C1-C2 linkage.
Peptide Bond Planarity
Partial double bond character due to resonance restricts rotation, forcing a planar configuration around the amide bond.
Vitamin Solubility Logic
Fat-soluble (A, D, E, K) accumulate in liver/adipose tissue; Water-soluble (B, C) are excreted and require daily intake.
Enzyme Specificity 'Lock and Key'
Active site complementarity; non-covalent interactions (Van der Waals, H-bonds) drive substrate binding specificity.
Concept Collisions Used by Examiners
Competitive examinations rarely assess concepts in isolation. Instead, examiners intentionally combine multiple concepts from this and related chapters to create higher-order questions that test conceptual reasoning, analytical thinking, and problem-solving ability. The concept collision patterns below represent the combinations most frequently used while designing questions for this chapter.
Exam Coverage
Understand how this chapter is tested across major competitive examinations.
JEE Advanced
India · Competitive Exam · Undergraduate
JEE Main
India · Competitive Exam · Undergraduate
BITSAT
India · Competitive Exam · Undergraduate
NEET-UG
India · Competitive Exam · Undergraduate
IISER Aptitude Test (IAT)
India · Competitive Exam · Undergraduate
NEST
India · Competitive Exam · Undergraduate
NSEC
India · Olympiad · High School
AP Chemistry
United States · Curriculum · Advanced Placement
A-Level Chemistry
United Kingdom · Curriculum · Advanced Level
Singapore A-Level Chemistry
Singapore · Curriculum · Advanced Level
Cambridge International A-Level Chemistry
International · Curriculum · Cambridge
International Chemistry Olympiad (IChO)
International · Olympiad · International
Practice Questions
Strengthen your understanding by solving carefully selected questions from this chapter.
D-Glucose is treated with excess \ce{CH3OH} in the presence of dry \ce{HCl} gas to yield compound (a mixture of anomers). Compound is then subjected to the following reaction sequence:
- \ce{HCN (aq)}, trace \ce{KCN}
- Dilute \ce{H3O+},
- \ce{Br2 / H2O}
Identify the major final product(s) of this sequence.
Pure -D-glucopyranose (specific rotation ) is dissolved in a dilute solution at and allowed to reach thermodynamic equilibrium. The final specific rotation of the mixture is observed to be . In a separate experiment, the same sugar in neutral reaches an equilibrium specific rotation of .
Which of the following statements correctly describes the sites of deuterium incorporation in the D-glucopyranose molecules isolated from the alkaline equilibrium mixture, and the relationship between and ?
Consider the reaction of the following four carbohydrate derivatives with an excess of phenylhydrazine () in an acetate buffer (pH ) at :
(I) D-Glucose (II) D-Fructose (III) 2-Deoxy-D-glucose (IV) Methyl -D-glucopyranoside
Let and be the number of equivalents of consumed per mole of I, II, III, and IV respectively, to form their final stable nitrogen-containing products and . Which of the following options correctly lists the values of and the correct structural relationship between the products?
D-Glucose exists in a catalytic solvent system at as an equilibrium mixture of - and -anomers. The standard free energy change for the mutarotation equilibrium () is .
Excess acetic anhydride is added to completely acetylate the glucose. Under these specific conditions, the rate of mutarotation is significantly faster than the rate of esterification, placing the reaction under Curtin-Hammett control.
The absolute free energy of the transition state () for the rate-determining step of the -anomer acetylation is lower than that of the -anomer acetylation.
Calculate the mole percentage of -D-glucopyranose pentaacetate in the final product mixture.
(Given: at , , )
Consider the behavior of D-glucopyranose () and the nucleoside uridine () in an aqueous buffer at and . While exhibits a time-dependent change in specific rotation (mutarotation), maintains a constant specific rotation. Which of the following statements correctly explains the fundamental stereoelectronic reason for the inability of to undergo mutarotation?
An equimolar mixture containing each of D-Glucose, D-Mannose, D-Fructose, D-Galactose, L-Glucose, and D-Allose is treated with an excess of phenylhydrazine () in an acetate buffer at until all reactions are complete. Let be the total number of moles of phenylhydrazine consumed, be the total number of structurally distinct osazones formed, and be the total number of moles of aniline () produced as a byproduct. Calculate the value of .
D-Arabinose undergoes Kiliani-Fischer chain extension (1. , 2. , ) to yield two diastereomeric aldohexoses, and . Upon dissolution in water at 298 K, both and undergo mutarotation to reach their respective anomeric equilibria. For epimer , the -pyranose form is thermodynamically dominant (). For epimer , the -pyranose form is thermodynamically dominant (). Identify and , and the primary stereochemical reason for the anomalous anomeric equilibrium of .
A pure sample of the protected tripeptide \ce{N-acetyl-L-threonyl-L-isoleucyl-L-valinamide} is dissolved in an aqueous buffer at and heated at for an extended period. This leads to complete thermodynamic equilibration via base-catalyzed proton abstraction of all susceptible carbon atoms. Assuming no peptide bond cleavage, elimination reactions, or side-chain degradation occurs, what is the total number of stereoisomers of this molecule present in the final equilibrium mixture?
Consider the nucleoside 2'-deoxyguanosine dissolved in an aqueous buffer at pH 7.4 and 298 K. The system is allowed to reach thermodynamic equilibrium. Which of the following statements accurately describes the dynamic structural isomerism and stereochemistry of the molecule under these conditions?
A naturally occurring disaccharide (\ce{C12H22O11}) exhibits the following properties: I. It does not decolorize bromine water and fails to exhibit mutarotation in an aqueous solution at . II. Exhaustive methylation of with excess \ce{CH3I}/\ce{Ag2O} followed by dilute aqueous \ce{HCl} hydrolysis yields a single chiral carbohydrate derivative . III. Enzymatic hydrolysis of with yeast -glucosidase yields only D-glucose, whereas emulsin (-glucosidase) produces no reaction.
Identify the exact glycosidic linkage in and the IUPAC name of .
D-Arabinose undergoes a Kiliani-Fischer synthesis to yield two C2-epimeric aldohexoses, and . The aldohexose forms a -pyranose conformation in which all non-anomeric hydroxyl groups and the hydroxymethyl group are in equatorial positions.
Both and are independently subjected to the following reaction sequence:
- Excess , Pyridine
- in (yielding the thermodynamically stable -glycosyl bromide)
- , (Koenigs-Knorr glycosidation)
- Catalytic in (Zemplén deacetylation)
Let the final major isolated methyl glycosides obtained from and be and , respectively. Which of the following correctly identifies and ?
Consider the enzymatic hydrolysis of cellobiose () by the enzyme cellulase. The reaction proceeds rapidly at and , but ceases completely at . Evaluate the following six statements regarding the substrate, the enzyme, and the reaction thermodynamics:
I. Cellobiose contains a glycosidic linkage, which is a hemiacetal linkage that undergoes rapid mutarotation at , preventing enzyme recognition. II. The cessation of hydrolysis at is primarily due to the endothermic disruption of non-covalent interactions (e.g., hydrogen bonding, hydrophobic effects) within cellulase, altering its tertiary structure. III. The 'Lock and Key' specificity is lost at because the thermal energy exceeds the activation energy for the cleavage of the enzyme's primary peptide bonds. IV. The hydrolysis of cellobiose into two molecules of D-glucose is thermodynamically spontaneous () at both and . V. In the most stable chair conformation of the major product formed upon hydrolysis (in aqueous equilibrium), all hydroxyl groups and the hydroxymethyl group occupy equatorial positions. VI. Cellulase acts by lowering the activation energy of the hydrolysis, which simultaneously shifts the equilibrium constant () of the reaction towards the formation of D-glucose at .
How many of the above statements are CORRECT?
Consider the rare keto-enol tautomerization of the purine base Guanine () within a deoxyribonucleotide residue in a DNA strand at and physiological pH. Evaluate the following statements regarding its stereoelectronic properties and structural geometry:
I. In the enol tautomer (), the N1 atom transitions from a hydrogen bond donor to a hydrogen bond acceptor due to proton migration to the C6 oxygen. II. forms a stable mispair with Thymine () because the altered hydrogen-bonding profile perfectly complements the N3-H donor and C4=O acceptor of Thymine. III. The tautomeric shift alters the dipole moment and effective pairing distance, inducing a conformational shift of the -N-glycosidic linkage towards the \textit{syn} geometry to alleviate steric hindrance with the sugar-phosphate backbone. IV. The standard Gibbs free energy change () for the transition is highly negative, which drives the spontaneous formation of Z-DNA.
Which of the given statements are correct?
An unknown carbohydrate () exhibits the following chemical behavior: I. It does not reduce Tollens' reagent and fails to exhibit mutarotation in aqueous solution at . II. Upon heating with excess phenylhydrazine in an acetate buffer () at for 45 minutes, it yields a yellow crystalline osazone . III. Exhaustive methylation of using followed by mild acid hydrolysis yields two distinct tetra-O-methylated monosaccharides, and . IV. Structural analysis reveals that possesses exactly one primary methoxy group, whereas possesses exactly two primary methoxy groups.
Which of the following correctly identifies and the mechanistic rationale for the formation of ?
A synthetic non-reducing disaccharide is synthesized by linking the anomeric carbon of D-galactofuranose to the anomeric carbon of D-glucopyranose via an glycosidic bond.
\textbf{Experiment 1:} of is treated with an excess of periodic acid (\ce{HIO4}) in aqueous solution at . \textbf{Experiment 2:} of is subjected to mild acid hydrolysis (, ) until equilibrium is reached. The resulting solution is neutralized and then heated with an excess of Fehling's solution.
Let be the moles of \ce{HIO4} consumed in Experiment 1. Let be the moles of formic acid (\ce{HCOOH}) produced in Experiment 1. Let be the moles of formaldehyde (\ce{HCHO}) produced in Experiment 1. Let be the moles of \ce{Cu2O} precipitated in Experiment 2.
Determine the values of and .
An optically active \ce{D}-ketohexose gives a positive Tollens' test. In the alkaline medium of the reagent, undergoes the Lobry de Bruyn–van Ekenstein transformation via an intermediate to form an equilibrium mixture containing and two aldohexoses and . Oxidation of and with warm \ce{HNO3} yields aldaric acids and , respectively. It is observed that is optically inactive (meso) while is optically active. Which of the following correctly identifies , the intermediate , and the stereochemical relationship between and ?
A sample of D-arabinose () is dissolved in an aqueous buffer at and treated with of . The nucleophilic addition is allowed to reach completion. The resulting solution is immediately treated with an excess of Tollens' reagent () at . Assuming the cyanohydrin adducts do not undergo base-catalyzed reversion during the rapid Tollens' test, determine the mass of the silver precipitate formed and the stereochemical relationship of the newly formed cyanohydrin products. (Given: Atomic mass of )
Consider the non-standard amino acid 2-amino-3-(4-aminophenyl)propanoic acid (-aminophenylalanine) in an aqueous solution at 298 K. The values for its three ionizable groups are 2.0, 4.6, and 9.2. Calculate the isoelectric point (pI) of this amino acid.
L-Phenylalanine (Compound ) is reacted with excess in the presence of dry to form intermediate . Subsequent treatment of with excess acetic anhydride in the presence of pyridine at 298 K yields Compound . Let represent the partition coefficient defined as at pH 7.0. Let represent the melting point, and represent the molecular dipole moment. Which of the following correctly compares the physical properties of and ?
Consider two synthetic amino acids, and :
: 2-amino-3-(4-aminophenyl)propanoic acid : 2-amino-3-(2-aminophenyl)propanoic acid
For both and , the values of the and groups are 2.0 and 9.0, respectively. The values of the conjugate acids of the aromatic groups in and are 5.1 and 4.4 (not necessarily in that order).
A mixture of and is subjected to paper electrophoresis in a buffer at at .
Which of the following correctly describes the isoelectric points () and the direction of migration of and ?
An aqueous solution of L-Lysine ( for , for , for ) is reacted with an excess of D-glucose at 298 K. A selective Maillard reaction occurs, forming a Schiff base at the less sterically hindered and intrinsically more basic amino group of L-Lysine. The of the conjugate acid of the newly formed imine nitrogen is 3.50. Assuming the values of the unreacted groups remain unchanged and no other side reactions occur, what is the isoelectric point (pI) of the isolated Schiff base conjugate?
The tertiary structure of a globular enzyme is critically stabilized by a buried intramolecular salt bridge between a Glutamic acid residue (side chain ) and a Histidine residue (side chain ). Assuming the ionizations of these side chains are independent, the enzyme is subjected to a pH shift from its optimum pH (where the probability of the intact salt bridge is maximized) to a highly acidic pH of 2.0 at 298 K, resulting in irreversible denaturation due to the disruption of electrostatic interactions.
Determine the optimum pH for the salt bridge, the approximate percentage of the salt bridge that remains intact at pH 2.0, and the dominant electrostatic state of the (Glutamic acid, Histidine) side chains at pH 2.0, respectively.
An enzyme exhibits strict 'Lock and Key' specificity towards its substrate at in an aqueous buffer (). Upon severe thermal denaturation at elevated temperatures, the catalytic activity drops to zero. Beyond the disruption of non-covalent interactions (hydrogen bonds and van der Waals forces), what is the fundamental stereoelectronic cause for the irreversible loss of the active site's precise three-dimensional geometry?
An aqueous buffer solution at () contains a folded globular protein and a G-C rich double-stranded DNA (dsDNA). A high concentration of urea () is added to the solution. Which of the following statements correctly describes the primary structural changes and the underlying thermodynamic reasons?
A aqueous buffer solution at () contains of a native globular protein non-covalently bound to its prosthetic group, Vitamin C (Ascorbic acid, a monoprotic weak acid with ). To study the prosthetic group, of an immiscible organic solvent (1-octanol) is added, and the mixture is vigorously shaken. The low dielectric constant of 1-octanol disrupts the hydrophobic core of the protein, causing complete denaturation and precipitation at the interface, quantitatively releasing the Vitamin C. The released Vitamin C partitions between the aqueous and organic phases. Only the unionized form of Vitamin C () is soluble in the organic phase, with a distribution coefficient . Assuming the pH of the aqueous phase remains constant and the volumes are strictly additive, what is the total concentration of Vitamin C (in all its forms) remaining in the aqueous phase at equilibrium?
A biochemist is studying the thermal denaturation of a synthetic polypeptide at . The polypeptide exists in a functional Native state () and a Denatured state (), which are in rapid equilibrium. The denatured state further undergoes a secondary equilibrium to form a stable, inactive dimer aggregate (). The coupled equilibria are given as:
Initially, the polypeptide is prepared in a buffer such that the total monomeric concentration is (assuming initially). Once the system reaches thermodynamic equilibrium, what is the percentage of the original polypeptide that remains in the functional Native state ()?
An equimolar mixture containing each of D-glucose, D-mannose, D-fructose, D-galactose, D-talose, D-ribose, and sucrose is heated with an excess of phenylhydrazine in an aqueous acetate buffer (pH ) at until all possible reactions (including the complete hydrolysis of any susceptible glycosidic bonds) have gone to completion.
Let be the number of structurally distinct osazones formed in the final mixture. Let be the total number of moles of phenylhydrazine consumed. Let be the total number of moles of aniline produced as a byproduct.
Calculate the value of .
A non-reducing trisaccharide upon exhaustive methylation followed by strong acidic hydrolysis yields equimolar amounts of 2,3,4,6-tetra--methyl-D-galactose, 2,3,4-tri--methyl-D-glucose, and 1,3,4,6-tetra--methyl-D-fructose.
One mole of is subjected to mild acidic hydrolysis (, ) which selectively cleaves the most kinetically labile glycosidic linkage to form a monosaccharide and a disaccharide . The resulting mixture is then treated with excess phenylhydrazine in an acetate buffer (pH 4.5) at until osazone formation is complete.
Determine the total number of moles of phenylhydrazine consumed by the carbohydrate mixture per mole of .
An aldopentose upon oxidation with dilute yields an optically active aldaric acid. is subjected to Kiliani-Fischer synthesis (using , followed by hydrolysis and reduction) to yield two aldohexoses, and . Oxidation of with yields an optically inactive (meso) aldaric acid, whereas yields an optically active aldaric acid. and are then individually reacted with 3 equivalents of phenylhydrazine () at to form osazones and respectively. What is the relationship between and , and how many chiral centers are present in the osazone product?
A sample of an equimolar mixture of D-fructose and Guanine is treated with an excess of phenylhydrazine (\ce{PhNHNH2}) in an acetic acid buffer at . Assuming the reaction proceeds to completion, what is the total number of moles of phenylhydrazine consumed and the total number of moles of ammonia (\ce{NH3}) produced, respectively?
An enzyme utilizes the imidazole side chain of a Histidine residue (, , ) as a general base to catalyze the phosphorylation of Guanosine by ATP at . The reaction specifically targets the most sterically accessible hydroxyl group of the nucleoside's pentose sugar to form a nucleotide. During an in vitro experiment, the reaction buffer is acidified such that the ratio of the protonated to unprotonated imidazole side chain of the catalytic Histidine becomes . At this pH, the catalytic base is effectively 'shut off', and the nucleophilic attack on the phosphate donor is blocked. Identify the target esterification site on Guanosine and the net charge of the predominant Histidine species at this inhibited pH.
In an aqueous buffer at 298 K (pH = 7.4), the lactam-lactim (keto-enol) tautomerization equilibrium constant () for the nucleoside deoxyguanosine (dG) is . Upon phosphorylation to form deoxyguanosine 5'-monophosphate (dGMP), the negatively charged phosphate group exerts a through-space field effect. This effect selectively stabilizes the keto tautomer to minimize repulsive dipole-dipole interactions, increasing the standard free energy of tautomerization () by exactly .
Given at 298 K, determine the new tautomeric equilibrium constant () for the nucleotide. Additionally, identify the Hydrogen-Bond Donor (D) / Acceptor (A) profile at the Watson-Crick face (reading positions C6, N1, and C2 respectively) for the specific tautomer that is \textit{destabilized} by this field effect.
An enzyme, Uridine nucleosidase, specifically catalyzes the hydrolysis of the N-glycosidic linkage in Uridine to yield uracil and D-ribose at and . A researcher hypothesizes that Uridine-5'-monophosphate (UMP) will act as a strong competitive inhibitor for this enzyme due to its structural similarity to Uridine. Consider the following statements regarding this system:
I. The N-glycosidic linkage hydrolyzed by the enzyme in Uridine is a -linkage. II. UMP will effectively bind to the active site and significantly increase the apparent of the enzyme for Uridine without altering . III. The 5'-phosphate group of UMP exists predominantly as a dianion at , causing severe electrostatic repulsion and steric hindrance at the active site. IV. The 'Lock and Key' specificity of the enzyme relies on the unhindered, neutral 5'-OH group of the ribofuranose ring for proper active site fit.
How many of the above statements are correct?
2'-Deoxythymidine (initial concentration ) is reacted with a phosphoric acid buffer (total analytical concentration ) in a specialized solvent system at . The medium is buffered such that the concentration of neutral is exactly equal to the concentration of its monoanion (assume higher deprotonations are negligible).\n\nIn this medium, only the fully protonated, neutral species acts as the active electrophile for the nucleophilic acyl-like substitution by the nucleoside hydroxyl groups. The equilibrium constants for the formation of the 5'-phosphoester and 3'-phosphoester from neutral are and , respectively.\n\nTo drive the thermodynamically unfavorable phosphorylation, a molecular sieve apparatus continuously strips water, maintaining its steady-state concentration at . Assuming no other side reactions occur, what is the equilibrium concentration of the 5'-nucleotide (thymidine-5'-monophosphate)?
A biochemical mixture contains each of the following eight compounds in an aqueous solution at : (I) -D-Ribofuranose (II) Adenosine (III) Thymidine 5'-monophosphate (TMP) (IV) 2-Deoxy--D-ribofuranose (V) Maltose (VI) Sucrose (VII) Uridine (VIII) Lactose
What is the total number of compounds in this mixture that possess a free hemiacetal/hemiketal group, undergo mutarotation, and yield a silver mirror when treated with Tollens' reagent ()?
During DNA replication at , Thymine () typically exists in the lactam (keto) form and pairs with Adenine. However, a spontaneous point mutation can occur if undergoes tautomerization to its rare lactim (enol) form (), where the proton from N3 migrates to O4. In this form, it mispairs with a different standard nitrogenous base from the nucleotide pool.
Given that the of the N3-H proton in standard Thymine is , determine the following four parameters in order:
- The identity of the mispaired base .
- The total number of hydrogen bonds formed in the base pair.
- The number of hydrogen bond DONORS provided specifically by in this base pair.
- The net charge on the dominant species of standard Thymine at an alkaline pH of .
Consider a 1:1 aqueous complex of the DNA fragment and the dipeptide L-Histidyl-L-Lysine at 298 K. The initial pH of the buffer is 7.4.
The pH is gradually lowered to 1.0 and the mixture is heated, resulting in the complete acid-catalyzed hydrolysis of all amide, phosphodiester, and N-glycosidic linkages. Assume all resulting monomeric units (bases, sugars, and amino acids) remain structurally intact without further thermal degradation.
Given the values for the ionizable groups of the free amino acids: Histidine: -COOH (1.8), - (9.2), imidazole side-chain (6.0) Lysine: -COOH (2.2), - (9.0), - (10.5)
Identify the correct combination of: (i) The predominant net charge of the intact dipeptide at (prior to hydrolysis). (ii) The total moles of chiral organic molecules produced per mole of the complex. (iii) The total moles of inorganic phosphate () produced per mole of the complex.
An artificial electrophilic base analog, -nitrobenzenediazonium chloride, is incubated with 2'-deoxycytidine in an aqueous buffer at pH 8.5 and 273 K. Initially, a rapid reversible interaction is observed, but upon prolonged standing, a stable, irreversible covalent adduct is isolated, effectively bypassing standard DNA mismatch repair enzymes. Identify the structure of the major stable adduct and the dominant mechanistic control governing its formation.
A wild-type (WT) transcription factor binds to the major groove of a DNA double helix at and . The binding is driven by specific hydrogen bonds, yielding a standard enthalpy of binding and a standard entropy of binding . The protein's DNA-binding domain is a rigid -helix, constrained by the partial double-bond character of its peptide bonds.
A mutation introduces a highly flexible loop in the unbound protein, increasing its conformational entropy by compared to the WT unbound state. The enthalpy of the unbound state remains unchanged. To achieve the required 'Lock and Key' fit in the major groove, the mutant protein must adopt the exact same rigid bound conformation as the WT protein.
Calculate the standard free energy of binding () for the mutant protein at .
An aldopentose upon oxidation with dilute yields an optically active aldaric acid. undergoes Kiliani-Fischer chain extension to produce a mixture of two aldohexoses, and . The mixture of and is treated with excess phenylhydrazine () in an acetate buffer at to yield the osazone product(s) . Which of the following correctly describes the product(s) and the reaction stoichiometry?
D-Glyceraldehyde is subjected to the Kiliani-Fischer synthesis. The intermediate cyanohydrins are hydrolyzed and heated to yield a mixture of two stable cyclic compounds, and . Reduction of and with in water at pH 3-5 yields a mixture of two aldotetroses, and . The mixture of and is then treated with excess in the presence of catalytic dry to yield a mixture of major products .
Let be the number of compounds in the mixture that exhibit mutarotation in aqueous solution. Let be the number of compounds in the mixture that give a positive Tollens' test. Let be the total number of major stereoisomers present in the mixture .
Determine the correct set of values for .
D-Glyceraldehyde undergoes a Kiliani-Fischer chain extension via reaction with followed by complete hydrolysis using aqueous at to yield a mixture of epimeric aldonic acids. The unbranched aliphatic analog, butanoic acid, has a of at . Considering the intramolecular electronic effects in the newly formed aldonic acids, which of the following represents their most accurate estimated value at ?
D-Lyxose is subjected to the Kiliani-Fischer chain extension. The intermediate epimeric cyanohydrins are hydrolyzed and dehydrated to yield a mixture of two -lactones. To successfully isolate the corresponding aldohexoses, the lactones must be selectively reduced using Reagent . However, a student mistakenly treats the lactone mixture with excess in THF followed by aqueous acidic workup, resulting in a mixture of two alditols, and . Which of the following correctly identifies Reagent and the stereochemical nature of and ?
An optically active aldopentose undergoes the Kiliani-Fischer chain extension sequence: (i) , (ii) , , (iii) , pH 3-5. This yields a mixture of two aldohexoses, and . When and are separately heated with excess phenylhydrazine () in an acetate buffer at , they consume and moles of phenylhydrazine per mole of sugar, respectively, to form osazone derivatives and . Which of the following correctly describes the relationship between and , the values of and , and the number of chiral carbons in ?
An optically pure sample of -5-methyl-1,5-dihydro-2H-pyrrol-2-one is dissolved in excess containing a catalytic amount of and heated for a prolonged period at . After the system reaches thermodynamic equilibrium, the major tautomer present in the mixture is analyzed. Assuming no back-exchange of isotopes occurs during analysis, which of the following best describes the major isotopologue of this tautomer?
An aqueous solution containing of sucrose (, molar mass ) is completely hydrolyzed using dilute at . The resulting mixture is neutralized and treated with an excess of Tollens' reagent ( in aqueous ). Assuming complete oxidation of all reactive monosaccharides, what is the total mass of metallic silver deposited? (Atomic mass of )
An aqueous solution of a naturally occurring, non-reducing disaccharide () is hydrolyzed with dilute to yield a single D-aldohexose . forms an osazone identical to that formed by D-fructose. is subjected to the following reaction sequence: where and are isomeric aldoheptoses. Subsequent oxidation of and with warm concentrated yields heptaric acids and , respectively. Which of the following correctly describes the stereochemical relationship between and , and the optical activity of and ?
An aqueous solution contains an equimolar mixture (1 mole each) of four disaccharides: Sucrose, Lactose, Maltose, and Cellobiose. Four identical aliquots of this solution (each containing 1 mole of all four disaccharides) are subjected to different hydrolytic conditions at and optimal pH:
Aliquot I: Treated with Invertase (strictly specific to sucrose). Aliquot II: Treated with -galactosidase (strictly specific to -D-galactoside linkages). Aliquot III: Treated with Maltase (strictly specific to -(14)-D-glucosidic linkages). Aliquot IV: Heated with dilute aqueous \ce{H2SO4} until complete chemical hydrolysis occurs.
Assume all enzymatic and chemical hydrolyses proceed to 100% completion. Let be the total moles of free D-glucose molecules present in the final mixture of Aliquot . Let be the total moles of reducing sugar molecules present in the final mixture of Aliquot .
Calculate the value of .
An aqueous solution containing of sucrose and of lactose is subjected to complete acidic hydrolysis. The resulting mixture is then treated with an excess of phenylhydrazine in an acetate buffer (pH ) at until the reaction is complete. Let be the total moles of phenylhydrazine consumed, be the total moles of osazones formed, and be the number of structurally distinct osazones obtained. Identify the correct set of values for , , and .
One mole of a reducing disaccharide \ce{A} (), which yields only D-glucose upon complete acidic hydrolysis, is subjected to such hydrolysis. The resulting solution is neutralized and then treated with dilute \ce{Ba(OH)2} (aq) at 298 K until the Lobry de Bruyn-van Ekenstein equilibrium is established. The equilibrium mixture is found to contain exactly 30% D-fructose by mole fraction. The solution is then neutralized again and subjected to complete oxidative cleavage using excess \ce{HIO4} (aq). What is the total number of moles of formic acid (\ce{HCOOH}) and formaldehyde (\ce{HCHO}) produced, respectively?
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