🇮🇳 NEET MDS · subject
NEET MDS Biochemistry Syllabus
The Biochemistry syllabus for NEET MDS in full: 8 chapters, 23 topics and 75 sub-topics, every one listed below, plus 51 Biochemistry flashcards with answers.
Biochemistry syllabus: all 8 chapters
Expand any chapter to see its topics and sub-topics.
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Introduction to Biochemistry
2 topics- Scope and Importance
- Definition of Biochemistry
- Applications in Medicine
- Historical Development
- Cell Structure and Functions
- Cell Membrane
- Organelles
- Cytoskeleton
- Scope and Importance
-
Proteins
3 topics- Amino Acids
- Structure and Classification
- Essential and Non-Essential Amino Acids
- Peptide Bonds
- Protein Structure
- Primary Structure
- Secondary Structure
- Tertiary Structure
- Quaternary Structure
- Protein Function
- Enzymes
- Transport Proteins
- Structural Proteins
- Signaling Proteins
- Amino Acids
-
Enzymes
3 topics- Classification
- Oxidoreductases
- Transferases
- Hydrolases
- Lyases
- Isomerases
- Ligases
- Mechanism of Action
- Active Site
- Enzyme-Substrate Complex
- Catalytic Mechanisms
- Factors Affecting Enzyme Activity
- Temperature
- pH
- Substrate Concentration
- Inhibitors
- Classification
-
Carbohydrates
3 topics- Classification
- Monosaccharides
- Disaccharides
- Oligosaccharides
- Polysaccharides
- Metabolism
- Glycolysis
- Gluconeogenesis
- Glycogen Metabolism
- Pentose Phosphate Pathway
- Regulation
- Hormonal Regulation
- Allosteric Regulation
- Classification
-
Lipids
3 topics- Classification
- Fatty Acids
- Triglycerides
- Phospholipids
- Steroids
- Metabolism
- Beta-Oxidation
- Fatty Acid Synthesis
- Cholesterol Metabolism
- Lipoprotein Metabolism
- Clinical Aspects
- Hyperlipidemia
- Atherosclerosis
- Obesity
- Classification
-
Nucleic Acids
3 topics- DNA Structure and Function
- Double Helix
- DNA Replication
- DNA Repair
- RNA Structure and Function
- Types of RNA
- Transcription
- RNA Processing
- Gene Expression
- Genetic Code
- Translation
- Regulation of Gene Expression
- DNA Structure and Function
-
Vitamins and Minerals
3 topics- Fat-Soluble Vitamins
- Vitamin A
- Vitamin D
- Vitamin E
- Vitamin K
- Water-Soluble Vitamins
- Vitamin B Complex
- Vitamin C
- Minerals
- Macrominerals
- Microminerals
- Fat-Soluble Vitamins
-
Metabolism Integration
3 topics- Energy Balance
- ATP
- Energy Yield of Macronutrients
- Metabolic Pathways
- Catabolic Pathways
- Anabolic Pathways
- Hormonal Regulation
- Insulin
- Glucagon
- Thyroid Hormones
- Energy Balance
NEET MDS Biochemistry flashcards — 51 questions with answers
What is biochemistry and why is it important in dentistry?
Biochemistry is the study of chemical processes and molecules within living organisms. In dentistry it explains tooth/bone mineralization, salivary composition, caries, collagen of periodontium, and metabolic/nutritional disorders affecting oral health.
Name the four major classes of biomolecules in the human body.
Carbohydrates, lipids, proteins, and nucleic acids.
Which cell organelle is the 'powerhouse of the cell' and what is its main function?
The mitochondrion; it carries out oxidative phosphorylation to generate ATP via the electron transport chain and TCA cycle.
What is the function of the rough endoplasmic reticulum vs the smooth ER?
Rough ER (studded with ribosomes) synthesizes and folds secretory/membrane proteins; smooth ER synthesizes lipids/steroids, detoxifies drugs, and stores calcium.
What is the role of lysosomes in the cell?
Lysosomes are membrane-bound organelles containing acid hydrolases that digest intracellular and engulfed material (autophagy, phagocytosis); they function at an acidic pH (~5).
What model describes the structure of the plasma membrane?
The fluid mosaic model: a phospholipid bilayer with embedded integral and peripheral proteins that move laterally, with cholesterol and glycoproteins.
What is the general structure of an amino acid?
A central alpha-carbon bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom, and a variable side chain (R group).
How many standard amino acids exist and how are they grouped by R-group polarity?
20 standard amino acids, grouped as nonpolar (hydrophobic), polar uncharged, acidic (negatively charged), and basic (positively charged).
List the essential amino acids.
Phenylalanine, Valine, Threonine, Tryptophan, Isoleucine, Methionine, Histidine, Arginine (semi-essential), Leucine, Lysine (mnemonic: PVT TIM HALL).
What is the isoelectric point (pI) of an amino acid?
The pH at which the amino acid carries no net charge (exists as a zwitterion); pI = average of the two pKa values flanking the neutral species.
What is a peptide bond and which reaction forms it?
A peptide bond is an amide linkage between the carboxyl group of one amino acid and the amino group of another, formed by a dehydration (condensation) reaction.
Describe 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 a polypeptide; Quaternary = assembly of multiple subunits.
What bonds stabilize the tertiary structure of proteins?
Hydrogen bonds, hydrophobic interactions, ionic (salt) bridges, disulfide bonds, and van der Waals forces.
What is protein denaturation?
Loss of secondary, tertiary, and quaternary structure (without breaking peptide bonds) due to heat, pH, or chemicals, leading to loss of biological function.
Compare alpha-helix and beta-pleated sheet.
Alpha-helix: right-handed coil stabilized by intrachain H-bonds (e.g., keratin). Beta-sheet: extended strands stabilized by interchain/intrachain H-bonds, can be parallel or antiparallel (e.g., silk fibroin).
Give an example of a fibrous protein and a globular protein with their functions.
Fibrous: collagen (structural support in connective tissue, dentin, bone). Globular: hemoglobin (oxygen transport).
What is the function of hemoglobin and how does the Bohr effect affect it?
Hemoglobin transports O2 from lungs to tissues and CO2 back. Bohr effect: increased CO2/H+ (lower pH) decreases Hb's affinity for O2, promoting O2 release in tissues.
What are enzymes and what is their basic nature?
Enzymes are biological catalysts, mostly proteins (some RNA = ribozymes), that lower activation energy and accelerate reactions without being consumed.
What are the six IUBMB classes of enzymes?
Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, and Ligases.
What is the difference between a cofactor, coenzyme, and prosthetic group?
Cofactor = non-protein helper (metal ion or organic); Coenzyme = organic cofactor loosely bound (often vitamin-derived); Prosthetic group = cofactor tightly/covalently bound to the enzyme.
Show the other 31 Biochemistry flashcards
Explain the 'induced fit' model of enzyme action.
Substrate binding induces a conformational change in the active site so it molds around the substrate, optimizing catalysis (Koshland's model), unlike the rigid lock-and-key model.
What does the Michaelis-Menten constant (Km) represent?
Km is the substrate concentration at which reaction velocity is half of Vmax; a low Km indicates high enzyme-substrate affinity.
How do competitive and non-competitive inhibitors affect Km and Vmax?
Competitive: increases Km, Vmax unchanged. Non-competitive: Km unchanged, Vmax decreased.
How do temperature and pH affect enzyme activity?
Activity rises with temperature up to an optimum (~37°C) then falls due to denaturation; each enzyme has an optimum pH (e.g., pepsin ~2, alkaline phosphatase ~9) beyond which activity declines.
What is the difference between zero-order and first-order enzyme kinetics?
Zero-order: rate is independent of substrate concentration (enzyme saturated, at Vmax). First-order: rate is directly proportional to substrate concentration (low substrate).
How are carbohydrates classified?
Monosaccharides (glucose, fructose), disaccharides (sucrose, lactose, maltose), oligosaccharides, and polysaccharides (starch, glycogen, cellulose).
What is the net ATP yield of glycolysis and where does it occur?
Glycolysis occurs in the cytoplasm and yields a net 2 ATP and 2 NADH per glucose molecule, converting glucose to 2 pyruvate.
What is the role of the TCA (Krebs) cycle and where does it occur?
In the mitochondrial matrix, the TCA cycle oxidizes acetyl-CoA to CO2, producing 3 NADH, 1 FADH2, and 1 GTP per turn for energy generation.
How many ATP are produced from the complete oxidation of one glucose molecule?
Approximately 30-32 ATP (modern estimate) via glycolysis, TCA cycle, and oxidative phosphorylation.
What is the function of glycogenesis and glycogenolysis?
Glycogenesis = synthesis of glycogen from glucose (storage); glycogenolysis = breakdown of glycogen to release glucose, regulated by insulin (storage) and glucagon/epinephrine (breakdown).
What is gluconeogenesis and where does it occur?
Synthesis of glucose from non-carbohydrate sources (lactate, glycerol, glucogenic amino acids), mainly in the liver (and kidney) during fasting.
What is the main purpose of the HMP shunt (pentose phosphate pathway)?
To produce NADPH (for biosynthesis and antioxidant defense) and ribose-5-phosphate (for nucleotide synthesis); no ATP is generated.
How is blood glucose hormonally regulated?
Insulin lowers blood glucose (promotes uptake, glycogenesis); glucagon, epinephrine, cortisol, and growth hormone raise it (glycogenolysis, gluconeogenesis).
What are the clinical features of diabetes mellitus biochemically?
Hyperglycemia, glycosuria, ketonemia/ketonuria, polyuria, polydipsia, and elevated HbA1c due to insulin deficiency or resistance.
How are lipids classified?
Simple lipids (fats, oils, waxes), compound lipids (phospholipids, glycolipids, lipoproteins), and derived lipids (fatty acids, steroids, ketone bodies).
Where does fatty acid beta-oxidation occur and what does it yield?
In the mitochondrial matrix; each cycle removes 2 carbons producing 1 acetyl-CoA, 1 FADH2, and 1 NADH.
What are the three ketone bodies and when are they formed?
Acetoacetate, beta-hydroxybutyrate, and acetone; formed in the liver during starvation, fasting, or uncontrolled diabetes when fatty acid oxidation exceeds carbohydrate availability.
List the major lipoproteins in order of increasing density.
Chylomicrons, VLDL, IDL, LDL, HDL (density increases as protein content rises and lipid falls).
Why is LDL called 'bad' and HDL 'good' cholesterol?
LDL delivers cholesterol to tissues and promotes atherosclerosis; HDL performs reverse cholesterol transport, removing cholesterol from tissues to the liver.
What is the building block of DNA and its components?
The nucleotide: a nitrogenous base + deoxyribose sugar + phosphate group. Bases are adenine, guanine (purines), cytosine, thymine (pyrimidines).
Describe the Watson-Crick model of DNA structure.
A right-handed antiparallel double helix with a sugar-phosphate backbone; bases pair via H-bonds (A=T with 2 bonds, G≡C with 3 bonds) following Chargaff's rule.
What is the central dogma of molecular biology?
DNA → (transcription) → RNA → (translation) → Protein; information flows from DNA to RNA to protein (with reverse transcription as an exception).
Compare DNA and RNA.
DNA: deoxyribose, double-stranded, thymine, stores genetic info. RNA: ribose, usually single-stranded, uracil instead of thymine, involved in protein synthesis.
What are the three main types of RNA and their functions?
mRNA carries genetic code to ribosomes; tRNA brings amino acids during translation; rRNA forms the structural/catalytic core of ribosomes.
What is gene expression and its two main steps?
The process by which genetic information is used to synthesize a functional product (protein). Steps: transcription (DNA→mRNA) and translation (mRNA→protein).
List the fat-soluble vitamins and one deficiency disease for each.
A (night blindness/xerophthalmia), D (rickets/osteomalacia), E (hemolytic anemia/neuropathy), K (bleeding/poor clotting).
List the water-soluble vitamins and a key deficiency.
B1 (beriberi), B2, B3/niacin (pellagra), B5, B6, B7/biotin, B9/folate (megaloblastic anemia/neural tube defects), B12 (pernicious anemia), and C (scurvy).
Why is vitamin C important for dental and connective tissue health?
Vitamin C is a cofactor for prolyl/lysyl hydroxylase needed for collagen synthesis; deficiency causes scurvy with bleeding gums, poor wound healing, and weak dentin/bone.
What is the role of vitamin D and calcium/phosphate in mineralization?
Vitamin D (calcitriol) promotes intestinal absorption of calcium and phosphate, maintaining serum levels needed for hydroxyapatite formation in bones and teeth.
Name key macrominerals and trace elements and a function of each.
Macrominerals: calcium and phosphorus (bone/tooth mineralization), sodium/potassium (fluid balance). Trace: iron (hemoglobin), iodine (thyroid hormones), fluoride (enamel resistance to caries), zinc (enzyme cofactor).
What is BMR and how is energy balance defined?
Basal Metabolic Rate is the energy expended at complete rest to maintain vital functions. Energy balance = energy intake vs expenditure; positive balance causes weight gain, negative balance causes weight loss.
Same Biochemistry syllabus in other exams
The Biochemistry outline above is identical in these 2 exams:
NEET MDS Biochemistry FAQ
What is in the NEET MDS Biochemistry syllabus?
NEET MDS Biochemistry is split into 8 chapters: Introduction to Biochemistry, Proteins, Enzymes, Carbohydrates, Lipids, Nucleic Acids, Vitamins and Minerals and Metabolism Integration. Together they contain 23 topics and 75 sub-topics.
How many chapters are in NEET MDS Biochemistry?
8 chapters, containing 23 topics and 75 sub-topics. The largest chapter is Proteins, with 3 topics.
Are there flashcards for NEET MDS Biochemistry?
Yes — a 51-card Biochemistry 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.