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INI CET Bio Chemistry Syllabus
The Bio Chemistry syllabus for INI CET in full: 10 chapters, 32 topics and 99 sub-topics, every one listed below, plus 50 Bio Chemistry flashcards with answers.
Bio Chemistry syllabus: all 10 chapters
Expand any chapter to see its topics and sub-topics.
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Molecular Biology
5 topics- Structure and function of nucleic acids: DNA and RNA
- DNA replication
- Enzymes involved
- Replication fork
- Leading and lagging strands
- Transcription
- RNA polymerase
- mRNA synthesis
- Transcription factors
- Regulation
- Translation
- Ribosomes
- tRNA
- Codons
- Initiation
- Elongation
- Termination
- Regulation
- Genetic code
- Codons
- Amino acids
- Start and stop codons
- Wobble hypothesis
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Proteins
5 topics- Amino acids
- Classification
- Structure
- Properties
- Essential vs. non-essential amino acids
- Protein structure
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure
- Protein folding and stability
- Chaperones
- Denaturation
- Refolding
- Enzymes
- Classification
- Mechanism of enzyme action
- Kinetics
- Enzyme regulation
- Enzyme inhibitors
- Competitive inhibitors
- Non-competitive inhibitors
- Mixed inhibitors
- Amino acids
-
Carbohydrate Metabolism
5 topics- Glycolysis
- Pathway
- Enzymes
- Regulation
- Energetics
- Gluconeogenesis
- Pathway
- Substrates
- Enzymes
- Regulation
- Pentose Phosphate Pathway
- Functions
- Significance
- Glycogen Metabolism
- Synthesis
- Degradation
- Regulation
- Citric Acid Cycle (Krebs Cycle)
- Steps
- Enzymes
- Regulation
- Metabolic Significance
- Glycolysis
-
Lipid Metabolism
4 topics- Fatty acid metabolism
- β-oxidation
- Synthesis
- Desaturation
- Elongation
- Triacylglycerol metabolism
- Synthesis
- Breakdown
- Regulation
- Lipoprotein metabolism
- Classification
- Structure
- Functions
- Role in lipid transport
- Ketone bodies
- Synthesis
- Utilization
- Regulation
- Fatty acid metabolism
-
Amino Acid Metabolism
3 topics- Overview of amino acid metabolism
- Transamination
- Deamination
- Urea cycle
- Metabolism of specific amino acids
- Glucogenic vs. ketogenic amino acids
- One-carbon metabolism
- Methylation reactions
- Folate metabolism
- Vitamin B12
- Overview of amino acid metabolism
-
Bioenergetics and Oxidative Phosphorylation
3 topics- ATP synthesis
- Chemiosmotic hypothesis and mitochondrial electron transport chain
- Regulation of oxidative phosphorylation
- Mitochondrial disorders and their biochemical basis
- ATP synthesis
-
Intermediary Metabolism
2 topics- Regulation of metabolic pathways
- Hormonal regulation
- Allosteric regulation
- Covalent modification
- Integration of metabolism
- Metabolic interconversions
- Metabolic flux
- Energy balance
- Regulation of metabolic pathways
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Hormones and Signal Transduction
2 topics- Hormone classification
- Endocrine vs. exocrine hormones
- Peptide hormones
- Steroid hormones
- Mechanisms of action
- Signal transduction pathways
- Second messengers
- G-proteins
- Protein kinases
- Gene regulation
- Hormone classification
-
Nutrition and Vitamins
2 topics- Essential Nutrients
- Macronutrients (carbohydrates, proteins, fats)
- Micronutrients (vitamins, minerals)
- Functions, Sources, and Deficiencies of Vitamins
- Fat-soluble vitamins (A, D, E, K)
- Water-soluble vitamins (B-complex, C)
- Essential Nutrients
-
Biochemical Techniques
1 topic- Principles and applications of biochemical techniques
- Spectrophotometry
- Chromatography
- Electrophoresis
- PCR
- DNA sequencing
- Recombinant DNA technology
- Principles and applications of biochemical techniques
INI CET Bio Chemistry flashcards — 50 questions with answers
What are the structural differences between DNA and RNA?
DNA has deoxyribose sugar, is usually double-stranded, and uses thymine; RNA has ribose sugar (2'-OH), is usually single-stranded, and uses uracil instead of thymine.
Which base pairs form in DNA and how many hydrogen bonds hold each?
Adenine pairs with Thymine via 2 hydrogen bonds; Guanine pairs with Cytosine via 3 hydrogen bonds. GC-rich DNA is therefore more stable (higher melting temperature).
In which direction is a new DNA strand synthesized, and why is one strand discontinuous?
Synthesis is always 5' to 3'. Because the two parental strands are antiparallel, the leading strand is made continuously while the lagging strand is made discontinuously as Okazaki fragments.
What is the function of DNA helicase, primase, and DNA ligase in replication?
Helicase unwinds the double helix; primase synthesizes RNA primers to start synthesis; DNA ligase seals nicks between Okazaki fragments by forming phosphodiester bonds.
What is the role of RNA polymerase in transcription, and does it require a primer?
RNA polymerase synthesizes RNA from a DNA template in the 5'-to-3' direction; unlike DNA polymerase, it does NOT require a primer to initiate.
Name the three main types of RNA and their roles in protein synthesis.
mRNA carries the genetic message (codons); tRNA brings amino acids and reads codons via its anticodon; rRNA forms the catalytic core of the ribosome.
What are the three stages of translation?
Initiation (ribosome assembles at the start codon), elongation (peptide bonds form as the ribosome moves along mRNA), and termination (release at a stop codon).
Which ribosomal activity catalyzes peptide bond formation, and what is unusual about it?
Peptidyl transferase activity catalyzes peptide bond formation; it is a ribozyme, meaning the catalyst is rRNA (RNA), not protein.
What are the start and stop codons of the standard genetic code?
The start codon is AUG (codes for methionine); the stop codons are UAA, UAG, and UGA.
What are the key features of the genetic code (degeneracy, universality, non-overlapping)?
It is degenerate (multiple codons per amino acid), nearly universal, non-overlapping, comma-less, and read as triplet codons in a fixed reading frame.
How are amino acids classified by R-group polarity?
Nonpolar/hydrophobic, polar uncharged, acidic (negatively charged: Asp, Glu), and basic (positively charged: Lys, Arg, His).
Which amino acids are essential in humans?
Phenylalanine, Valine, Threonine, Tryptophan, Isoleucine, Methionine, Histidine, Arginine, Leucine, Lysine (mnemonic: PVT TIM HALL).
Define the four levels of protein structure.
Primary: amino acid sequence; Secondary: local folding (alpha-helix, beta-sheet) via H-bonds; Tertiary: overall 3D fold of one chain; Quaternary: assembly of multiple subunits.
What bonds stabilize the tertiary structure of a protein?
Hydrophobic interactions, hydrogen bonds, ionic (salt) bridges, and covalent disulfide bonds between cysteine residues.
What is the role of molecular chaperones in protein folding?
Chaperones (e.g., heat-shock proteins like Hsp70) assist correct folding and prevent aggregation of partially folded polypeptides, without being part of the final structure.
What is an enzyme and how does it speed up reactions?
An enzyme is a biological catalyst (usually protein) that lowers the activation energy of a reaction by stabilizing the transition state, without being consumed.
Define Km and Vmax in Michaelis-Menten kinetics.
Vmax is the maximum reaction velocity at saturating substrate; Km is the substrate concentration at half Vmax and reflects enzyme-substrate affinity (low Km = high affinity).
How do competitive, non-competitive, and uncompetitive inhibitors affect Km and Vmax?
Competitive: increases apparent Km, Vmax unchanged. Non-competitive: Km unchanged, Vmax decreased. Uncompetitive: both Km and Vmax decreased.
What is the net ATP and NADH yield of glycolysis per glucose?
Net gain of 2 ATP (4 produced minus 2 used) and 2 NADH, plus 2 pyruvate molecules.
Which enzyme is the key irreversible regulatory (rate-limiting) step of glycolysis?
Phosphofructokinase-1 (PFK-1); it is activated by AMP and fructose-2,6-bisphosphate and inhibited by ATP and citrate.
Show the other 30 Bio Chemistry flashcards
What is the purpose of gluconeogenesis, and where does it primarily occur?
It synthesizes glucose from non-carbohydrate precursors (lactate, glycerol, glucogenic amino acids) to maintain blood glucose; mainly in the liver (and kidney).
What are the two main products and purposes of the Pentose Phosphate Pathway?
NADPH (for reductive biosynthesis and antioxidant defense) and ribose-5-phosphate (for nucleotide synthesis); the rate-limiting enzyme is glucose-6-phosphate dehydrogenase.
Which enzymes carry out glycogen synthesis and breakdown, and what regulates them?
Glycogen synthase builds glycogen; glycogen phosphorylase breaks it down. Glucagon/epinephrine (via cAMP-PKA) activate phosphorylase and inhibit synthase; insulin reverses this.
What enzyme deficiency causes von Gierke disease (Type I glycogen storage disease)?
Glucose-6-phosphatase deficiency, causing severe fasting hypoglycemia, hepatomegaly, and lactic acidosis.
What are the net products of one turn of the Citric Acid (Krebs) cycle per acetyl-CoA?
3 NADH, 1 FADH2, 1 GTP (or ATP), and 2 CO2.
Which enzyme is the rate-limiting step of the Krebs cycle?
Isocitrate dehydrogenase; the cycle is also regulated at citrate synthase and alpha-ketoglutarate dehydrogenase, inhibited by high ATP/NADH.
How are fatty acids activated and transported into the mitochondria for beta-oxidation?
Fatty acids are activated to fatty acyl-CoA, then carried across the inner mitochondrial membrane by the carnitine shuttle (carnitine palmitoyltransferase I and II).
What does each round of fatty acid beta-oxidation produce?
Each cycle removes a 2-carbon acetyl-CoA and yields 1 FADH2 and 1 NADH, shortening the fatty acid chain by two carbons.
What is the structure of a triacylglycerol and the rate-limiting enzyme of its breakdown?
A glycerol backbone esterified to three fatty acids; hormone-sensitive lipase is the rate-limiting enzyme of lipolysis (stimulated by glucagon/epinephrine).
What are the major lipoprotein classes ranked by density, and what do chylomicrons and LDL carry?
Chylomicrons < VLDL < IDL < LDL < HDL (increasing density). Chylomicrons carry dietary triglycerides; LDL carries cholesterol to tissues ('bad'); HDL returns cholesterol to liver ('good').
What are ketone bodies, where are they made, and when are they produced?
Acetoacetate, beta-hydroxybutyrate, and acetone, synthesized in the liver mitochondria (ketogenesis) during prolonged fasting/starvation or uncontrolled diabetes; the liver cannot use them (lacks thiophorase).
How is the amino group removed from amino acids before their carbon skeletons are metabolized?
By transamination (transferring the amino group to alpha-ketoglutarate forming glutamate) followed by oxidative deamination of glutamate by glutamate dehydrogenase, releasing ammonia.
What enzyme defect causes phenylketonuria (PKU) and what is the consequence?
Deficiency of phenylalanine hydroxylase (or its BH4 cofactor) prevents conversion of phenylalanine to tyrosine, causing phenylalanine accumulation and intellectual disability if untreated.
What is one-carbon metabolism and which vitamins/carrier are central to it?
Transfer of single-carbon units (methyl, methylene, formyl) for synthesis of purines, thymidylate, and methionine; it relies on tetrahydrofolate (from folate) and vitamin B12, with SAM as the major methyl donor.
Where do the electrons from NADH and FADH2 enter the electron transport chain, and what is the final electron acceptor?
NADH enters at Complex I and FADH2 at Complex II; oxygen (O2) is the final electron acceptor, being reduced to water.
Explain the chemiosmotic theory of ATP synthesis.
Electron transport pumps protons into the intermembrane space, creating an electrochemical gradient; protons flow back through ATP synthase (Complex V), driving phosphorylation of ADP to ATP.
How do uncouplers like 2,4-dinitrophenol affect oxidative phosphorylation?
They dissipate the proton gradient by carrying protons across the inner membrane, so electron transport continues but ATP synthesis stops and energy is released as heat.
Why are mitochondrial disorders often multisystem and maternally inherited?
Mitochondrial DNA is inherited from the mother, and tissues with high energy demand (brain, muscle, heart) are most affected; defects impair oxidative phosphorylation (e.g., MELAS, LHON, Leigh syndrome).
What is meant by integration of metabolism in the fed (absorptive) state?
High insulin promotes glucose uptake, glycogen synthesis, lipogenesis, and protein synthesis, while inhibiting gluconeogenesis and lipolysis, storing fuel.
How is metabolism integrated during fasting/starvation?
Glucagon dominates: glycogenolysis then gluconeogenesis maintain blood glucose, lipolysis and beta-oxidation supply energy, and ketone bodies fuel the brain to spare glucose and protein.
How are hormones classified by chemical structure?
Peptide/protein hormones (e.g., insulin), steroid hormones (e.g., cortisol), and amino-acid derivatives (e.g., thyroxine, epinephrine).
How do steroid hormones differ from peptide hormones in their mechanism of signaling?
Lipophilic steroid hormones cross the membrane and bind intracellular/nuclear receptors to alter gene transcription; hydrophilic peptide hormones bind cell-surface receptors and act via second messengers.
What is the cAMP second messenger signal transduction pathway?
Hormone binds a GPCR, activating Gs protein, which stimulates adenylate cyclase to produce cAMP, which activates protein kinase A (PKA) to phosphorylate target proteins.
What are the major classes of essential nutrients the body cannot synthesize adequately?
Essential amino acids, essential fatty acids (linoleic and alpha-linolenic acid), vitamins, minerals, and water (plus dietary energy from carbohydrates/fats).
Which deficiencies cause scurvy, beriberi, and pellagra?
Scurvy from vitamin C deficiency; beriberi from vitamin B1 (thiamine) deficiency; pellagra from vitamin B3 (niacin) deficiency (the 3 Ds: dermatitis, diarrhea, dementia).
Which vitamin deficiency causes night blindness, and which causes rickets/osteomalacia?
Vitamin A deficiency causes night blindness (xerophthalmia); vitamin D deficiency causes rickets in children and osteomalacia in adults.
What does vitamin B12 (cobalamin) deficiency cause, and what is its main dietary source?
Megaloblastic (pernicious) anemia with subacute combined degeneration of the spinal cord; sourced from animal products and requires intrinsic factor for absorption.
What is the principle of electrophoresis as a biochemical technique?
Charged molecules (proteins, nucleic acids) migrate through a gel in an electric field; separation is based on charge, size, and shape (e.g., SDS-PAGE separates proteins mainly by molecular weight).
What is the principle behind ELISA?
Enzyme-Linked Immunosorbent Assay uses antigen-antibody specificity with an enzyme-linked antibody that produces a measurable color change, used to detect and quantify proteins/antigens or antibodies.
What does the Lambert-Beer law describe in spectrophotometry?
Absorbance is directly proportional to the concentration of the absorbing substance and the path length (A = epsilon x c x l), allowing quantification of solutes by light absorption.
Same Bio Chemistry syllabus in other exams
The Bio Chemistry outline above is identical in these 3 exams:
INI CET Bio Chemistry FAQ
What is in the INI CET Bio Chemistry syllabus?
INI CET Bio Chemistry is split into 10 chapters: Molecular Biology, Proteins, Carbohydrate Metabolism, Lipid Metabolism, Amino Acid Metabolism, Bioenergetics and Oxidative Phosphorylation, Intermediary Metabolism, Hormones and Signal Transduction, Nutrition and Vitamins and Biochemical Techniques. Together they contain 32 topics and 99 sub-topics.
How many chapters are in INI CET Bio Chemistry?
10 chapters, containing 32 topics and 99 sub-topics. The largest chapter is Molecular Biology, with 5 topics.
Are there flashcards for INI CET Bio Chemistry?
Yes — a 50-card Bio Chemistry deck, printed in full in the flashcards section of this page and available in the Examius app with spaced repetition. The free plan covers one exam of your choice, including its flashcards; Examius Pro, a one-time purchase, unlocks every other exam and deck.