1. General Biochemistry A. Chemical Basis of Life Atoms Elements in the human body Chemical bonds Water pH and buffers Biological importance of water B. Biomolecules Carbohydrates Lipids Proteins Nucleic acids Vitamins Minerals

Reading File

Asking for Preferences

Finding Sources

Reading File

Finding Sources

Reading File

Finding Sources

Reading File

Finding Sources

Reading File

Here is a comprehensive, MBBS-level explanation of the entire General Biochemistry curriculum you listed, drawn from Ganong's Review of Medical Physiology (26th ed.), Lippincott's Illustrated Biochemistry (8th ed.), and Basic Medical Biochemistry - A Clinical Approach (6th ed.).

General Biochemistry: Complete Study Notes for MBBS

SECTION A: Chemical Basis of Life

1. Atoms

An atom is the smallest unit of an element that retains the chemical properties of that element. It consists of:

Nucleus: contains protons (positively charged) and neutrons (no charge)
Electron cloud: electrons (negatively charged) orbit the nucleus in shells

Key definitions:

Atomic number = number of protons (defines the element)
Atomic mass = protons + neutrons
Isotopes = atoms of the same element with different numbers of neutrons (e.g., ¹²C vs ¹⁴C). Radioactive isotopes are used in medical imaging and research.
Ions = atoms that have gained or lost electrons, giving them a net charge (e.g., Na⁺, Cl⁻, Ca²⁺)

Moles and molecular weight (clinically important): A mole is the gram-molecular weight of a substance - 1 mole = 6 × 10²³ molecules. The dalton (Da) is 1/12th the mass of carbon-12; proteins are typically expressed in kilodaltons (kDa). The milliequivalent (mEq) is used for charged particles in body fluids - one equivalent = 1 mol of ion divided by its valence. For example, 1 mEq of Ca²⁺ = 40g ÷ 2 = 20g. This is critical in electrolyte management in clinical medicine. - Ganong's Review of Medical Physiology, p. 16

2. Elements in the Human Body

The human body is made of approximately 26 elements, but just 4 account for ~96% of body mass:

Element	Symbol	% Body Mass	Key Role
Oxygen	O	~65%	Water, oxidative metabolism
Carbon	C	~18%	Backbone of all organic molecules
Hydrogen	H	~10%	Water, organic molecules
Nitrogen	N	~3%	Amino acids, nucleic acids

Other important elements (trace but essential):

Calcium (Ca²⁺): bone, muscle contraction, signal transduction
Phosphorus (P): ATP, nucleic acids, bone mineral (hydroxyapatite)
Potassium (K⁺): major intracellular cation; resting membrane potential
Sodium (Na⁺): major extracellular cation; osmolality, action potential
Magnesium (Mg²⁺): cofactor for >300 enzymes; ATP stabilization
Iron (Fe): hemoglobin (O₂ transport), cytochromes (electron transport)
Iodine (I): thyroid hormone synthesis
Zinc, Copper, Selenium, Cobalt: enzyme cofactors and structural roles

3. Chemical Bonds

Bonds are the forces holding atoms together in molecules.

a) Covalent Bonds

Electrons are shared between atoms
Strong bonds: require significant energy to break
Can be single (C-C), double (C=C), or triple (C≡C)
Polar covalent: unequal sharing (e.g., O-H in water; O is more electronegative)
Nonpolar covalent: equal sharing (e.g., C-H bonds)

b) Ionic Bonds

Complete transfer of electrons between atoms
Create oppositely charged ions that attract each other (e.g., Na⁺...Cl⁻)
Weak in aqueous solutions (water disrupts them)

c) Hydrogen Bonds

Electrostatic attraction between a partially positive H (bonded to N or O) and a partially negative N or O of another molecule
Individually weak (~1/20th of covalent bond) but collectively very strong in large numbers
Critical for: DNA double-helix stability, protein secondary structure (α-helices, β-sheets), and water's unique properties

d) Van der Waals Forces

Very weak, transient attractions between adjacent nonpolar molecules due to momentary charge fluctuations
Important in hydrophobic interactions (lipid bilayer stability)

e) Disulfide Bonds

Covalent bonds between the -SH groups of two cysteine residues → -S-S-
Important for protein tertiary/quaternary structure stabilization
Example: insulin has 3 disulfide bonds - Lippincott's Biochemistry, p. 27

4. Water

Water (H₂O) is the solvent of life. Its unique properties derive from its polar nature and hydrogen bonding capacity.

Structure: The oxygen atom pulls electrons away from the two hydrogen atoms, creating a dipole moment. The molecule is V-shaped (bent), with a partial negative charge on O and partial positive charges on each H.

Properties of biological importance (Ganong's, p. 123):

Property	Basis	Biological Significance
High surface tension	H-bonds	Maintains fluid surfaces (e.g., alveolar lining)
High heat of vaporization	H-bonds	Sweating effectively cools the body
High heat capacity	H-bonds	Resists temperature changes; stabilizes body temperature
High dielectric constant	Polarity	Excellent solvent for ions and polar molecules
Osmotic properties	Solvent	Drives osmosis across membranes

Osmosis: When water is separated from a solution by a semipermeable membrane, water molecules diffuse down their concentration gradient into the solution. The pressure needed to stop this movement is the osmotic pressure (P = nRT/V). Osmolarity is expressed in milliosmoles (mOsm). Normal plasma osmolality = 285-295 mOsm/kg. - Ganong's, p. 223

Electrolytes (e.g., NaCl) dissociate in water into their cation and anion forms. Key electrolytes: Na⁺, K⁺, Ca²⁺, Mg²⁺, Cl⁻, HCO₃⁻. Their differential distribution across membranes creates membrane potential and drives action potentials. - Ganong's, p. 131

5. pH and Buffers

pH is the negative logarithm of the hydrogen ion concentration:

pH = -log[H⁺]

pH 7.0 = neutral (pure water at 25°C)
pH < 7.0 = acidic; pH > 7.0 = alkaline
Normal blood pH: 7.35-7.45 (slightly alkaline)
Gastric fluid: ~pH 3.0; Pancreatic secretion: ~pH 8.0

Each pH unit represents a 10-fold change in [H⁺].

Acids and Bases:

Acid = proton (H⁺) donor: HA → H⁺ + A⁻
Base = proton acceptor
Strong acids/bases (e.g., HCl, NaOH): fully dissociate
Weak acids/bases: partially dissociate; more physiologically relevant

Henderson-Hasselbalch Equation:

pH = pKₐ + log([A⁻]/[HA])

pKₐ = negative log of the dissociation constant
Buffering is most effective when pH ≈ pKₐ (i.e., when [A⁻]/[HA] = 1)

Biological Buffers (Ganong's, p. 148):

Bicarbonate buffer (CO₂/HCO₃⁻) - most important in plasma
- H₂CO₃ ⇌ H⁺ + HCO₃⁻
- pKₐ = 6.1; effective because CO₂ is regulated by lungs and HCO₃⁻ by kidneys
Phosphate buffer (H₂PO₄⁻/HPO₄²⁻) - important in urine and intracellular fluid; pKₐ = 6.8
Protein buffer - histidine residues act as H⁺ acceptors; hemoglobin is a major blood buffer
Ammonia buffer - in the renal tubules

Isohydric Principle: All buffer pairs in a homogeneous solution are in equilibrium with the same [H⁺], so studying one buffer tells you about all.

Clinical Acid-Base Disorders:

Acidosis (pH < 7.35) and Alkalosis (pH > 7.45) impair O₂ delivery and CO₂ removal
Types: Respiratory (CO₂ problem) or Metabolic (HCO₃⁻ problem)

6. Biological Importance of Water

Water serves multiple critical biological roles:

Universal solvent: Dissolves ions, polar molecules, and gases → enables chemical reactions
Reactant and product: Hydrolysis (digestion) and condensation (synthesis) reactions
Transport medium: Blood plasma (~92% water) transports nutrients, O₂, hormones, waste
Temperature regulation: High heat capacity and heat of vaporization buffer temperature changes
Lubrication: Synovial fluid, cerebrospinal fluid, pleural fluid
Structural role: Maintains cell turgor; contributes to tissue architecture
Osmotic balance: Regulates cell volume and extracellular fluid volume
Ionization: Water ionizes to H⁺ + OH⁻ (Kw = 10⁻¹⁴ at 25°C), establishing pH

SECTION B: Biomolecules

1. Carbohydrates

Carbohydrates are organic molecules with the empirical formula (CH₂O)n - equal amounts of carbon and water. They are the primary fuel source of the body. - Ganong's, p. 707

Classification:

Class	Definition	Examples	Notes
Monosaccharides	Single sugar unit	Glucose, Fructose, Galactose (hexoses); Ribose, Deoxyribose (pentoses)	Cannot be hydrolyzed further
Disaccharides	2 monosaccharides	Sucrose (Glu+Fru), Lactose (Glu+Gal), Maltose (Glu+Glu)	Joined by glycosidic bonds
Oligosaccharides	3-10 sugar units	Present on glycoproteins, glycolipids	Cell signaling, cell recognition
Polysaccharides	>10 sugar units	Glycogen (storage, animals), Starch (storage, plants), Cellulose (structural, plants)	Digested or serve structural roles

Glucose is the principal monosaccharide in the body and the brain's primary fuel. Most monosaccharides are D-isomers. Glucose exists in ring form (pyranose) in solution.

Glycoproteins: Sugar moieties attached to proteins aid in cellular targeting, receptor recognition, and immune identity (e.g., ABO blood groups). - Ganong's, p. 709

Key metabolic pathway - Glycolysis: Glucose → 2 Pyruvate + 2 ATP (net) in the cytoplasm. Pyruvate enters the Krebs cycle under aerobic conditions.

Galactosemia (clinical): Congenital deficiency of galactose-1-phosphate uridyl transferase leads to galactose accumulation → serious growth disturbances. Treatment: galactose-free diet. - Ganong's, p. 803

Fructose metabolism: Fructose-2,6-bisphosphate is an important regulator of hepatic gluconeogenesis. High levels stimulate glycolysis; low levels facilitate gluconeogenesis.

2. Lipids

Lipids are a diverse group of hydrophobic or amphipathic molecules. They are not polymers but are grouped by their common property of solubility in nonpolar solvents. - Ganong's, p. 820

Major classes:

a) Fatty Acids

Long chains of carbon with a terminal carboxyl group (-COOH)
Saturated: No double bonds (e.g., palmitic acid C16:0, stearic acid C18:0) - solid at room temperature
Unsaturated: One or more double bonds (e.g., oleic acid C18:1, linoleic C18:2) - liquid at room temperature
Naturally occurring fatty acids have an even number of carbon atoms
Essential fatty acids: Cannot be synthesized by humans; must be dietary (linoleic acid ω-6, α-linolenic acid ω-3)

b) Triglycerides (Triacylglycerols)

3 fatty acids esterified to glycerol
Primary form of fat storage in adipose tissue
Major energy reserve (9 kcal/g vs 4 kcal/g for carbohydrates/proteins)

c) Phospholipids

Glycerol backbone + 2 fatty acids + phosphate group + polar head group
Amphipathic (hydrophobic tail + hydrophilic head) → form bilayer membranes
Examples: phosphatidylcholine (lecithin), phosphatidylserine, phosphatidylinositol
Phosphatidylinositol-4,5-bisphosphate (PIP₂) is an important cell signaling molecule

d) Cholesterol and Sterols

Steroid ring structure; important membrane component
Precursor for bile acids, steroid hormones (cortisol, estrogen, testosterone), and vitamin D
Transported in blood as lipoproteins (LDL, HDL, VLDL)

e) Sphingolipids

Contain sphingosine backbone; important in neuronal membranes
Deficiency of enzymes breaking them down → lysosomal storage diseases (e.g., Gaucher, Niemann-Pick, Tay-Sachs)

f) Eicosanoids

Derived from 20-carbon polyunsaturated fatty acids (arachidonic acid)
Include prostaglandins, thromboxanes, leukotrienes
Mediate inflammation, fever, pain, platelet aggregation

Fatty Acid Oxidation (β-oxidation): Fatty acids are broken down 2 carbons at a time in the mitochondria → acetyl-CoA → Krebs cycle → ATP. Long-chain fatty acids must be transported via the carnitine shuttle across the inner mitochondrial membrane. - Ganong's, p. 825

3. Proteins

Proteins are the most abundant and functionally diverse molecules in living systems. They are linear polymers of amino acids. - Lippincott's Biochemistry, p. 24

A. Amino Acids - the Building Blocks

20 standard amino acids encoded by DNA
General structure: central α-carbon bonded to:
- Amino group (-NH₃⁺ at physiological pH)
- Carboxyl group (-COO⁻ at physiological pH)
- Hydrogen atom
- R group (side chain) - defines the amino acid

Classification by R group:

Category	Examples	Characteristics
Nonpolar/aliphatic	Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine	Hydrophobic; form protein core
Aromatic	Phenylalanine, Tyrosine, Tryptophan	Absorb UV light (useful in protein detection)
Polar uncharged	Serine, Threonine, Cysteine, Asparagine, Glutamine	Participate in H-bonds
Positively charged	Lysine, Arginine, Histidine	Protonated at physiological pH
Negatively charged	Aspartate, Glutamate	Deprotonated at physiological pH

Special amino acids:

Proline: has a secondary amino group; disrupts α-helices; important in collagen
Cysteine: forms disulfide bonds (-S-S-); critical in active sites
Glycine: smallest, no chirality; fits tight spaces (collagen every 3rd residue)
Histidine: pKₐ ~6.0; acts as H⁺ buffer at physiological pH → important in hemoglobin buffering

Nonstandard amino acids: formed by post-translational modification (e.g., hydroxyproline in collagen requires vitamin C)

B. Levels of Protein Structure

Primary structure: Linear sequence of amino acids held by peptide bonds (covalent). Determines all higher-order structure. Mutations here cause disease (e.g., sickle cell disease: Glu→Val at position 6 of β-globin). - Lippincott's, p. 490
Secondary structure: Local folding patterns stabilized by hydrogen bonds between backbone atoms:
- α-helix: right-handed coil; 3.6 residues per turn; H-bond between C=O of residue n and N-H of residue n+4
- β-pleated sheet: parallel or antiparallel strands; H-bonds between strands
- Turns and loops: connect these elements
Tertiary structure: Overall 3D folding of a single polypeptide chain. Stabilized by:
- Hydrophobic interactions (nonpolar R groups cluster in core)
- Hydrogen bonds
- Ionic bonds (salt bridges)
- Disulfide bonds (between cysteines)
- Van der Waals forces
Quaternary structure: Association of two or more polypeptide chains (subunits). Example: Hemoglobin (2α + 2β subunits).

C. Protein Functions

Function	Example
Enzymes (catalysts)	Hexokinase, pepsin, DNA polymerase
Transport	Hemoglobin (O₂), albumin (fatty acids, drugs)
Structural	Collagen, keratin, actin, tubulin
Hormones	Insulin, glucagon, growth hormone
Antibodies (immune)	IgG, IgM
Receptors	Insulin receptor, β-adrenergic receptor
Contractile	Myosin, actin
Storage	Ferritin (iron), myoglobin (O₂ in muscle)

D. Metabolic Functions of Amino Acids

Glucogenic amino acids → converted to glucose (e.g., alanine, glutamine)
Ketogenic amino acids → converted to ketone bodies (e.g., leucine, lysine)
Amino acids are precursors for: thyroid hormones, catecholamines, histamine, serotonin, melatonin, heme, creatine, and glutathione
Methionine provides the methyl group (via S-adenosylmethionine/SAM) for synthesis of epinephrine, creatine, and methylated DNA - Ganong's, p. 702

Urea Cycle: NH₄⁺ from amino acid deamination is converted to urea in the liver (ornithine → citrulline → arginine → urea + ornithine). Consumes 3 ATP. Liver failure → hyperammonemia (elevated NH₃). - Ganong's, p. 696

4. Nucleic Acids

Nucleic acids carry and express genetic information. There are two types: DNA and RNA.

Building blocks - Nucleotides (Ganong's, p. 507):

Each nucleotide = Nitrogenous base + Sugar + Phosphate group

Nitrogenous bases:

Purines (double ring): Adenine (A), Guanine (G) - present in both DNA and RNA
Pyrimidines (single ring): Cytosine (C) - both; Thymine (T) - DNA only; Uracil (U) - RNA only

Sugars:

DNA: deoxyribose (lacks -OH at 2' carbon)
RNA: ribose (has -OH at 2' carbon)

Phosphodiester backbone: Nucleotides are linked 3'→5' via phosphodiester bonds, giving the chain polarity (5' end and 3' end).

Phosphate groups make DNA and RNA negatively charged (hence "nucleic acids"). - Lippincott's, p. 4351

DNA (Deoxyribonucleic Acid) - Ganong's, p. 500

Found in nucleus, mitochondria, and bacteria
Double-stranded anti-parallel helix
Base pairing (Watson-Crick): A=T (2 H-bonds), G≡C (3 H-bonds)
Helix dimensions: ~2.0 nm diameter; 3.4 nm per full turn (10 base pairs/turn)
Has major and minor grooves (important for protein-DNA interactions)
DNA is compacted by association with histones → nucleosomes → chromosomes
Diploid human cell: 46 chromosomes (~3 billion base pairs)
A gene = DNA sequence encoding one polypeptide (may produce multiple proteins by alternative splicing)

RNA (Ribonucleic Acid)

Generally single-stranded
Types and functions:

Type	Abbreviation	Function
Messenger RNA	mRNA	Carries genetic code from DNA to ribosome
Transfer RNA	tRNA	Brings amino acids to ribosome; anticodon matches codon
Ribosomal RNA	rRNA	Structural + catalytic component of ribosomes
Small nuclear RNA	snRNA	RNA splicing (removal of introns)
MicroRNA	miRNA	Post-transcriptional gene regulation

Central Dogma: DNA → (Transcription) → RNA → (Translation) → Protein

Translation: Proteins are synthesized by ribosomes reading mRNA in codons (3 nucleotides = 1 amino acid). - Tietz Textbook, p. 1552

Clinical relevance - Gout:

Purines are degraded via xanthine to uric acid by xanthine oxidase. Excess uric acid deposits as monosodium urate crystals in joints → gout. Treatment: allopurinol (inhibits xanthine oxidase), colchicine (inhibits phagocytosis of crystals). - Ganong's, p. 495

5. Vitamins

Vitamins are organic micronutrients that the body cannot synthesize in adequate amounts and must obtain from the diet. They function primarily as enzyme cofactors and regulatory molecules.

Classification:

Fat-Soluble Vitamins (A, D, E, K)

Absorbed with dietary fat; stored in fat and liver; can cause toxicity if excess.

Vitamin	Active Form	Function	Deficiency
A (Retinol)	Retinal, Retinoic acid	Vision (rhodopsin formation), epithelial differentiation, immune function	Night blindness, xerophthalmia, keratomalacia
D (Cholecalciferol)	1,25-(OH)₂D₃ (Calcitriol)	Ca²⁺ and PO₄³⁻ absorption; bone mineralization	Rickets (children), Osteomalacia (adults)
E (Tocopherol)	α-tocopherol	Antioxidant; protects cell membranes from lipid peroxidation	Hemolytic anemia, peripheral neuropathy
K (Phylloquinone)	Hydroquinone	Carboxylation of clotting factors (II, VII, IX, X) and proteins C and S	Bleeding disorder, prolonged PT

Water-Soluble Vitamins (B-complex and C)

Not stored (except B₁₂); regular dietary intake required.

Vitamin	Coenzyme Form	Function	Deficiency
B₁ (Thiamine)	TPP (Thiamine pyrophosphate)	Pyruvate dehydrogenase, α-ketoglutarate dehydrogenase	Beriberi (wet: cardiac; dry: neurological), Wernicke-Korsakoff (alcoholism)
B₂ (Riboflavin)	FAD, FMN	Electron carriers in oxidative phosphorylation	Glossitis, cheilosis, photophobia
B₃ (Niacin)	NAD⁺, NADP⁺	Electron carriers (redox reactions); over 400 reactions	Pellagra (4 D's: Dermatitis, Diarrhea, Dementia, Death)
B₅ (Pantothenate)	Coenzyme A (CoA)	Acetyl-CoA synthesis; fatty acid metabolism	Very rare; fatigue, paresthesia
B₆ (Pyridoxine)	Pyridoxal phosphate (PLP)	Transamination, decarboxylation; heme synthesis; neurotransmitter synthesis	Peripheral neuropathy, sideroblastic anemia
B₇ (Biotin)	Biocytin	Carboxylation reactions (pyruvate carboxylase, acetyl-CoA carboxylase)	Dermatitis, alopecia (raw egg whites bind biotin)
B₉ (Folate)	Tetrahydrofolate (THF)	One-carbon transfer; purine & pyrimidine synthesis; methionine synthesis	Megaloblastic anemia; neural tube defects (pregnancy)
B₁₂ (Cobalamin)	Methylcobalamin, Adenosylcobalamin	Folate regeneration; myelin synthesis; odd-chain fatty acid metabolism	Megaloblastic anemia + subacute combined degeneration of spinal cord
C (Ascorbate)	Ascorbic acid	Collagen hydroxylation (prolyl/lysyl hydroxylase); antioxidant; iron absorption	Scurvy (bleeding gums, perifollicular hemorrhages, poor wound healing)

Key note on B₁₂ and Folate: B₁₂ deficiency causes the "folate trap" - folate gets stuck as 5-methylTHF and cannot be used. Both cause megaloblastic anemia, but only B₁₂ deficiency causes neurological damage. - Robbins, p. 997

6. Minerals

Minerals are inorganic micronutrients required for structural and functional roles. They serve as cofactors, structural components, and electrolytes.

Macrominerals (required in large amounts >100 mg/day):

Mineral	Key Functions	Deficiency	Sources
Calcium (Ca²⁺)	Bone/teeth (99% of body Ca); muscle contraction; signal transduction; coagulation	Tetany, osteoporosis, rickets	Dairy, leafy greens
Phosphorus (P)	Bone/teeth; ATP; nucleic acids; phospholipids	Rare; muscle weakness, hemolytic anemia	Meat, dairy, legumes
Potassium (K⁺)	Major intracellular cation; resting membrane potential (-70 mV); cardiac rhythm	Hypokalemia: muscle weakness, arrhythmias	Bananas, potatoes
Sodium (Na⁺)	Major extracellular cation; osmolality; nerve impulse; Na⁺/K⁺-ATPase	Hyponatremia: confusion, seizures	Table salt
Magnesium (Mg²⁺)	Cofactor for >300 enzymes; ATP-Mg complex; DNA repair	Hypomagnesemia: tetany, arrhythmias	Nuts, whole grains
Chloride (Cl⁻)	Acid-base balance; HCl in stomach	Rare; metabolic alkalosis	Table salt

Trace Minerals (required in small amounts):

Mineral	Key Functions	Deficiency
Iron (Fe)	Hemoglobin (heme); myoglobin; cytochromes; catalase	Iron-deficiency anemia (most common nutritional deficiency worldwide): microcytic hypochromic anemia
Iodine (I)	Thyroid hormones (T₃, T₄) synthesis	Hypothyroidism, goiter; cretinism (fetal)
Zinc (Zn)	>100 metalloenzymes; immune function; wound healing; taste/smell	Growth retardation, hypogonadism, poor wound healing, dysgeusia
Copper (Cu)	Ceruloplasmin; cytochrome c oxidase; dopamine β-hydroxylase	Anemia, neurodegeneration; Wilson's disease = excess copper
Fluoride (F)	Bone and tooth enamel hardening	Dental caries; excess causes fluorosis
Selenium (Se)	Glutathione peroxidase (antioxidant)	Keshan disease (cardiomyopathy)
Cobalt (Co)	Component of vitamin B₁₂	Indirectly through B₁₂ deficiency

Clinical note on Iron: Iron deficiency is difficult to detect early because clinical signs appear only after iron stores are depleted. Serum ferritin is the best marker of iron stores; TIBC rises and serum iron falls in deficiency. - Medical Physiology, p. 3310

Summary Table: Biomolecules at a Glance

Biomolecule	Monomer	Bond linking monomers	Key functions
Carbohydrates	Monosaccharides	Glycosidic bond	Energy (glucose), storage (glycogen), structure (cellulose), signaling
Lipids	Fatty acids + glycerol	Ester bond	Energy storage, membranes, hormones, signaling
Proteins	Amino acids	Peptide bond	Enzymes, structural, transport, hormones, antibodies
Nucleic acids	Nucleotides	Phosphodiester bond	Genetic information (DNA), gene expression (RNA)

Sources:

Ganong's Review of Medical Physiology, 26th Edition - Chapter 1 (General Biochemistry)
Lippincott's Illustrated Biochemistry, 8th Edition - Units I, II (Proteins, Amino Acids)
Basic Medical Biochemistry - A Clinical Approach, 6th Edition - Sections I (Fuel Metabolism), Structure of Nucleic Acids
Robbins & Cotran Pathologic Basis of Disease - Chapter 9 (Vitamin C/Nutritional Diseases)
Medical Physiology (Boron & Boulpaep) - Chapter on Nutrition and Minerals

This is a shared conversation. Sign in to Orris to start your own chat.