Protein Classification and Structure

• Proteins are classified by function and structure.

Protein Classification

• Enzymes catalyze biochemical reactions, like amylase.
• Transport proteins carry molecules or ions; hemoglobin transports oxygen.
• Contractile proteins enable movement; actin and myosin in muscle cells.
• Structural proteins provide support and strength; collagen in skin and tendons.
• Antibodies neutralize foreign substances; viruses and bacteria
• Toxins protect organisms like snake venoms.
• Regulatory proteins control metabolism and nerve transmission, like insulin and parathyroid hormone.
• Nutrient proteins store nutrients, such as casein in milk and ovalbumin in egg whites.

Hierarchy of Protein Structure

• Proteins have four levels of structural organization: primary, secondary, tertiary, and quaternary.
• Primary structure is the linear sequence of amino acids in a polypeptide chain, determined by peptide bonds from the N-terminal (amino end) to the C-terminal (carboxyl end).
• Secondary structure involves localized folding patterns, stabilized by hydrogen bonds between the peptide backbone.
• α-Helix is a right-handed coil with 3.6 amino acids per turn, stabilized by hydrogen bonds between C=O of one peptide bond and N-H of another four residues away.
• β-Sheet: Polypeptide chains lie adjacent, forming hydrogen bonds between strands that can be parallel or antiparallel.
• Tertiary structure is the overall 3D shape of a single polypeptide chain, stabilized by interactions between side chains like hydrogen bonds, hydrophobic interactions, disulfide bonds, and electrostatic interactions; determines the protein’s function.
• Quaternary structure involves the association of multiple polypeptide chains (subunits) into a functional protein, stabilized by non-covalent interactions, such as hemoglobin (4 subunits) and insulin (2 subunits).

Shapes and Configurations of Proteins

• Fibrous proteins are long, insoluble fibers or sheets that provide structural support, like collagen in connective tissue and keratin in hair and wool.
• Collagen is a triple helix of three polypeptide chains, rich in proline and hydroxyproline. Every third residue is glycine, allowing tight packing, and stabilized by hydrogen bonds and covalent cross-links between lysine and histidine residues.
• Globular proteins are compact, spherical, and water-soluble, performing functional roles like enzymes and transporters.
• Myoglobin is a single-chain protein with a heme group binding oxygen, containing 8 α-helices and no β-sheets; polar side chains are on the surface, nonpolar side chains inside.

Factors Stabilizing Protein Structure

• Non-covalent interactions involve hydrogen bonds between polar side chains, hydrophobic interactions where nonpolar side chains cluster together, electrostatic interactions between oppositely charged side chains like lysine and glutamate, and disulfide bonds.
• Covalent bonds include peptide bonds linking amino acids in the primary structure and disulfide bonds stabilizing tertiary and quaternary structures.

Denaturation of Proteins

• Denaturation is the loss of a protein's 3D structure, caused by: heat disrupts hydrogen bonds and hydrophobic interactions, pH changes alter ionization, detergents disrupt hydrophobic interactions, urea/guanidinium chloride disrupts hydrogen bonds.
• Denaturation can sometimes be reversed.

Myoglobin and Hemoglobin

• Myoglobin is a monomeric protein that stores oxygen in muscle cells, contains a single heme group binding one oxygen with a hyperbolic oxygen-binding curve.
• Hemoglobin is a tetrameric protein with two α and two β chains, each with a heme group that binds oxygen cooperatively (sigmoidal oxygen-binding curve).
• The Bohr Effect is when hemoglobin releases oxygen more readily in acidic conditions (high CO₂).
• 2,3-Bisphosphoglycerate (BPG) binds to deoxyhemoglobin, reducing its oxygen affinity and promoting release.

Abnormal Hemoglobins

• Sickle-cell anemia is caused by a mutation in the β-chain of hemoglobin (glutamate → valine), leading to insoluble fibers when deoxygenated and causing sickle-shaped red blood cells; symptoms include blockage of blood flow, anemia, and pain.
• Hb M Iwate involves histidine → tyrosine, leading to methemoglobin (cannot bind oxygen).
• Hb Milwaukee involves valine → glutamate, stabilizing Fe(III) and preventing oxygen binding.

Fetal Hemoglobin (Hb F)

• Structure: Two α and two γ chains (α₂γ₂).
• Function: Higher affinity for oxygen than adult hemoglobin (Hb A), aiding oxygen transfer from mother to fetus.
• BPG Binding: Weaker binding to BPG than Hb A, further increasing oxygen affinity.

Carbon Monoxide Poisoning

• CO binds to hemoglobin more tightly than oxygen, preventing oxygen transport, causing dizziness, confusion, coma, and death.

Introduction to Proteins

• Proteins are chains of amino acids linked by peptide bonds, vital for life, found in skin, muscles, hair, blood, organs, and bones.
• Proteins are the second most abundant substance in the body after water.
• The sequence of amino acids determines the 3D structure, defining its function in a way that allows proteins to be flexible, stable, and degradable by cellular enzymes.

Categories of Proteins

• Fibrous proteins are found in animals and serve structural roles such as collagen in tendons and keratin in hair and nails and are insoluble in water.
• Globular proteins are typically water-soluble, performing functional roles like transport (hemoglobin) and enzymatic activity.

Protein Dynamics and Ligand Binding

• Proteins interact with ligands through non-covalent interactions: hydrogen bonds, electrostatic attractions, and hydrophobic interactions.
• The binding site on a protein is a cavity formed by amino acid side chains that fit the ligand like a "hand in a glove."
• To achieve effective binding, many weak interactions must occur simultaneously.

Functions of Proteins

• Growth and maintenance: Proteins build, maintain, and repair tissues.
• Enzymes: Catalyze biochemical reactions for digestion and energy production.
• Hormones: Act as chemical messengers, such as insulin regulating blood sugar.
• Structural support: Provide strength and elasticity, such as collagen in skin and bones.
• Transport: Carry molecules and ions, like hemoglobin transports oxygen.
• Immune Function: Antibodies defend against pathogens.
• Energy source: Proteins are used for energy when carbohydrates and fats are depleted.

Structure of Proteins

• Primary structure is a linear sequence of amino acids in a polypeptide chain.
• Secondary structure consists of localized folding patterns (α-helices, β-sheets), stabilized by hydrogen bonds.
• Tertiary structure is the overall 3D shape of a single polypeptide chain, stabilized by interactions between side chains.
• Quaternary structure is the association of multiple polypeptide chains into a functional protein, like hemoglobin with four subunits.

Protein Classification by Biological Function

• Enzymatic proteins catalyze biochemical reactions.
• Structural proteins provide support and strength like keratin and collagen.
• Transport proteins carry molecules and ions like hemoglobin.
• Nutrient and storage proteins store nutrients like casein in milk.
• Contractile proteins enable movement like actin and myosin in muscles.
• Defense proteins protect against pathogens like antibodies.
• Regulatory proteins control cellular and metabolic activities like hormones, such as insulin.
• Toxic proteins harm other organisms like snake venom.

Protein Sources

• Animal sources: Meat, poultry, fish, eggs, and dairy products provide complete proteins containing all essential amino acids.
• Plant sources: Nuts, grains, fruits, and vegetables provide incomplete proteins lacking one or more essential amino acids. To obtain all essential amino acids, vegetarians should combine different plant proteins.

Protein Requirements

• The Recommended Dietary Allowance (RDA) for protein is 0.8 grams per kilogram of body weight daily.
• For an average sedentary man, 56 grams/day is recommended.
• For an average sedentary woman, 46 grams/day is recommended.
• Essential amino acids: There are 9 amino acids obtained only from diet.

Protein Deficiency and Excess

• Protein deficiency:
  • Marasmus represents severe energy deficiency.
  • Kwashiorkor signifies severe protein deficiency.
  • Both are forms of Protein-Energy Malnutrition (PEM), the most widespread malnutrition globally.
• Protein excess:
  • Overconsumption leads to health risks such as heart or kidney disease, and bone loss.

Immunoglobulins (Antibodies)

• Immunoglobulins (antibodies) defend against foreign organisms by binding to antigens.
• The types of Immunoglobulins include:
  • IgG: Most abundant in blood, involved in secondary immune responses.
  • IgM: The first antibody produced in response to an infection.
  • IgA: Found in secretions, provides initial immune protection.
  • IgE: Involved in allergic reactions and parasite defense.
  • IgD: Regulates immune cell activation.

Collagen: A Fibrous Protein

• Collagen is the most abundant protein in the human body.
• It provides structural support in connective tissues.
• It's a triple helix of three polypeptide chains, rich in proline and hydroxyproline; every third residue is glycine.
• Vitamin C is essential for collagen synthesis: Deficiency leads to scurvy, characterized by poor wound healing, bleeding gums, and lethargy.

Myoglobin and Hemoglobin

• Myoglobin is a single-chain protein that stores oxygen in muscle cells, contains a heme group that binds oxygen with a hyperbolic oxygen-binding curve.
• Hemoglobin is a tetrameric protein with two α and two β chains, each containing a heme group, binds oxygen cooperatively with a sigmoidal oxygen-binding curve.
• The Bohr Effect shows that hemoglobin releases oxygen more readily in acidic conditions.
• 2,3-Bisphosphoglycerate (BPG) binds to deoxyhemoglobin, reducing its oxygen affinity and promoting oxygen release.

Fetal Hemoglobin (HbF)

• Structure: Two α and two γ chains (α₂γ₂).
• Function: Higher affinity for oxygen than adult hemoglobin (Hb A), aiding oxygen transfer from mother to fetus.
• BPG Binding: Weaker binding to BPG than Hb A, further increasing oxygen affinity.

Abnormal Hemoglobins

• Sickle-cell anemia involves a mutation in the β-chain of hemoglobin (glutamate → valine), leading to insoluble fibers when deoxygenated which causes sickle-shaped red blood cells with a variety of symptoms.
• Hb M Iwate signifies histidine → tyrosine, leading to methemoglobin, which cannot bind oxygen.
• Hb Milwaukee involves valine → glutamate, stabilizes Fe(III), preventing oxygen binding.

Carbon Monoxide Poisoning

• CO binds to hemoglobin more tightly than oxygen, preventing oxygen transport, leading to dizziness, confusion, coma, and death.

Post-Translational Modifications (PTMs)

• Post-translational modifications are covalent modifications occurring after protein synthesis, altering folding, conformation, stability, activity, localization, and interactions that enable proteins to respond to developmental signals and alter their function.

Types of Post-Translational Modifications

- Phosphorylation: Addition of a phosphate group to serine, threonine, or tyrosine, regulated cell cycle, growth, apoptosis, and signal transduction pathways, protein kinases add phosphate with ATP, and phosphatases remove phosphate groups.
- Glycosylation: Attachment of oligosaccharides to asparagine, serine, or threonine, affecting folding, conformation, distribution, stability, and function with N-linked glycans, O-linked glycans, phosphoglycans, and C-linked glycans.
- Ubiquitination: Attachment of ubiquitin to target proteins, marking them for destruction which is involved in cell cycle regulation, proliferation, differientiation, apoptosis, DNA repair, and immune responses.
- S-Nitrosylation: Addition of a nitrosyl (NO) group to cysteine residues, forming S-nitrothiols, stabilizing proteins and regulates gene expression.
-  Methylation: Addition of a methyl group to lysine or arginine, regulating chromatin structure and gene expression.
- N-Acetylation: Addition of an acetyl group to the nitrogen of lysine residues, regulating transcription factors, molecular chaperones, and cytoskeletal proteins; KATs adds groups and HDACs remove acetyl groups.
- Lipidation: Attachment of lipid groups to proteins for cellular localization, membrane tethering, and protein-protein interactions; e.g., C-terminal Glycosyl Phosphatidylinositol (GPI) anchors proteins to the plasma membrane.
- Disulfide Bonding: Covalent bonds formed between two cysteine residues that contributes to protein folding and stability.
- Proteolysis: Cleavage of peptide bonds by proteases and is involved in antigen processing, apoptosis, and cell signaling.

Examples of PTMs

• Phosphorylation: O-phosphorylation at serine residues.
• Methylation: S-N-alkylation at lysine residues.
• N-Acetylation: 5-N-acylation at lysine residues.
• S-Nitrosylation: Formation of S-nitrothiols on cysteine residues.

Peptide Bond

• Amino acids are linked by peptide bonds (amide bonds) by dehydration reactions releasing a water molecule, resulting in a molecule with an N-terminal (free amino group) and a C-terminal end.
• Short chains (less than 50 amino acids) are called a peptides, while longer chains area polypeptides; each protein consists of one or more polypeptide chains.
• After amino acids are added to a polypeptide chain they are known as amino acid residues.

Formation of a Peptide Bond

• A peptide bond forms between the carboxyl group of one amino acid and the amino group of another via dehydration, yielding a rigid, planar structure with partial double-bond character that restricts rotation around the C-N bond.

Dipeptides and Beyond

• When two amino acids are linked, the product is a dipeptide, like alanylvaline.
• As more amino acids are added, the chain lengthens, and the prefix reflects the number of residues, e.g., tripeptide (3), tetrapeptide (4).

Characteristics of the Peptide Bond

• Partial Double Bond Character : The partial double bond character is caused by delocalization, and this restrics rotation around the C-N bond.
• Rotation Angles : Other polypeptide bonds rotate freely, the angle of rotation is called phi.
• Ramachandran Plot : The Ramachandran plot presents rotations and provides the regions for structures.

Biochemical Roles of Peptides

• Small peptides are less complex but play significant biochemical roles.
• Small-peptide hormones include oxytocin (uterine contractions and lactation) and vasopressin (water reabsorption).
• Small-peptide neurotransmitters include enkephalins that act in the brain, reducing pain.
• Small-peptide antioxidants include glutathione that functions as an antioxidant in most cells.

Glutathione

• Glutathione (GSH) is a tripeptide with the sequence γ-glutamyl-L-cysteinylglycine that contains an unusual peptide bond between the γ-carboxyl group of glutamate and the amino group of cysteine.

Protein Turnover and Protein Degradation

• Protein turnover involves the continuous process of protein synthesis and degradation within cells that maintains cellular homeostasis.
• Protein synthesis occurs through translation using ribosomes, tRNA, and mRNA.
• Protein Degradation Pathways : Protein degradation occurs through the use of proteolysis.
• Faulty or damaged proteins are degraded into amino acids through different compartments, they are known as protein degradation pathways.

Body Protein Pool

• Factors that influence the protein pool include the rates synthesis and degradation, diet, and metabolism and nitrogen balance.

Location of Protein Degradation

• Dietary proteins are hydrolyzed into amino acids.
• Intracellular proteins degraded by proteasomes are marked by ubiqutin.
• Protein are also bygraded by lysosomes, which contains enzymes used for hydrolization.

Proteolysis

• Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids by polypeptide cleavage.
• Limited proteolysis involves specific peptide bond cleavage, and a product is synthesized with new functions.
• Complete degradation occurs when multiple sites are cleavd.

Proteases

• Enzymes that catalyze proteolysis are clasified as:
  • Exopeptidases involve near cleavage.
  • Endopeptidases (Proteinases) internal peptic bonds.

Lysosomal Protein Breakdown

• Lysosomes consists of a membrane with enzymes, proteins can then digested through endocytosis , and it allows degradation.

Ubiquitin-Dependent Protein Breakdown

• In eukaryotic cells proteins are degraded by the ubiquitin-proteasome pathway, also ubiquitin acts as a tag protein.
• Ubiquitin Activation : Ubiquitin is activated by enzyme. Ubiquitin Conjugation in this stage ubiquitin is transfered to another enzyme. Ubiquitin Ligation the other enzyme transferes ubiquitin, and these two moleculse create polyubiquination.

Introduction to Enzymes.

• Enzymes are biological catalysts that speed up biochemical reactions, mainly globular proteins with tertiary and quaternary structures.

Structure of Enzymes

• Catalytic and binding sites are present in the enzymes surface and that is know as an active site.
• Enzyme-substrate complexes are formed.

Co-factors

• They are required for enzymes activity and they are separated in inorganic, organic, and prosthetic groups.

Substrate

• Biochemical is also known as a substrate.
• During binding there is created enzyme-substrate complex.

Sites of Enzyme Synthesis

• Translation is responsible for protein synthesis and enzymes are synthesized in the ribosomes.

Intracellular and Extracellular Enzymes

• The cellular function is synthesized and retained in side the cell.
• Outside cell some digestive enzymes are produced, and this is know extracellular enzymes,

Characteristics of Enzymes

• Activation energy is reduced which causes reactions to speed up.
• Types of substrate is catalyzed by a enzyme.
• These molecules have sensitivity with changes to pH, temperature, and substrate concentration.
• Also molecule transformation of the enzyme can be achieved by the use of turnover number.

Nomenclature of Enzymes

• Based on the substrate enzymes acts on the are named,
• Also some enzymes are named before the conventions.

Classification of Enzymes

• Transfer chemical groups (e.g., hexokinase).
• Catalyze hydrolysis (e.g., lysozyme).
• Catalyze non-hydrolytic bond cleavage (e.g., fumarase).
• Catalyze intramolecular group transfer (e.g., triose phosphate isomerase).
• Catalyze synthesis of new covalent bonds using ATP (e.g., RNA polymerase).

Mechanism of Enzyme Action

• Processes at the Active Site enzymes are able to use bond strain, acid-base.

Enzyme Kinetics

• Substrat concentration and rate reaction is study known has enzyme kinetics.
• Michaelis-Menten rate enzyme-catalyzed reactions variation.
• V=Vmax[S] / Km+[S]
• Vmax is the most velocity, and Km is where it has maximum velocity.

Factors Affecting Enzyme Activity

• A denatured enzyme will have temperatures above of 35°C-45°C.
• Enzyme have values between 5-9° for their pH.
• Active sites or reaction rate is increased if substrate concentration is augmented.

Inhibition

• Enzyme inhibition is known as the reduction rate when inhibitor.
• Competitive inhibition.
• Uncompetitive inhibition where enzyme-substrate is bounded.
• Non-competitive inhibition binding to place where enzyme activity is reduced. -Irreversible Inhibition covalent binds permanently,

Activation

• Conversion of Enzyme Precursors: Trypsinogen to trypsin) are synthesized as inactive precursors enzymes.
• Co-factors: Such as Mg²⁺ or Zn²⁺ enzymes needs co-factors for activation.

Introduction to Enzyme Kinetics

• Enzymes are protein and biological catalysts this means they help with biochemical reactions.
• Also, we can view them as the reactions affected by the pH, temperature and also the substrate as well.

Key Concepts

• Binding and conversion of substrate takes at the active site.
• Enzymes can act on molecules.
• While binding them together can be formed a temp complex.
• It can be meausred also in moles per the unite of the substrate.

Michaeils-Menten Model

• Depends on the reaction of the substrate it can describe the reaction.
• The rate can be achieved when there is much substrate, and velocity is on the maximum, which is known as Vₘₐₓ
• Also the rate is in half of Vₘₐₓ which means the concentration is high known as Kₘ , also the low concentration of the other molecule makes is known as high affinity.
• The opposite is the similar has well, high Kₘ is know as low affinity.

Graphical Representions

• To achieve Lineweaver-Bruke with an equation which linearizes.
• Not so trusthworty due to data error. Also Eadie-Hofstee provides clearer representation.

Factors Affecting Enzyme Kinetics

• High increases the plateau so there is enzymes.
• Optimal temperature.
• Structure will be affected.
• If something decreases the shape of the enzymes their reaction increases.

Applications Of Enzyme Kinetics

• To desing effetive drugs kinetics and enzymes are to gether.
• Metabolic pathways, explains how they are regulated with KInetics Enzymes.
• By studying kinetics optimum uses in these industries is applied mostly in industries and biofuels.

Introduction to Lipids

• Hydrobon portion is high in molecules that are in organic solving, and the are lipids
• Energy is one thing that energy is high and in cell structure its stored known as signaling role.

Classifications of Lipids

• Open Chain Compounds (Saponifiable Lipids)
• Closed Chain Compounds (Non Saponifiable Lipids)
• Derived Lipids

Open chain Compounds (Saponifiable Lipids)

• Bonds that hold the molecules a hydrolysed.
  • • Fatty Acids building blocks.
  • • Triglycerides esters of the glicerol and acids.
  • • Phospholipids that c ontain posphate.
  • • Sphingolipids derived from sphingosine.
  • • Waxes esters from of alcoholes.

Closed chain Compounds (Non Saponifiable Lipids)

• Cant not by hydrolysed,
  • • Cholesterol important to membranes acids and hormones synthesis.
  • -Steroids like cortisol derived from esters.
  • • Steroids like cortisol and testosterone.

Derived Lipids

• A lipd that can be simple and is made by hydrolysis.
  • -Vitamin A
  • -Vitamin D
  • -Vitamin D

Fatty Acids

• They can be stored and they are fatty acids, and building blocks.
  • No found commonly in nature in but commonly from triglycerides
• Characterized by the eaven chains atoms, some of them are expections. Also can be saturated and carbon bonds

Fatty Acids types

• Only has one C-C bond.
• Exsample is Lauric acid, and Myristic acid
• Some chains do not bind
• Room temperature is commonly solid.
• One ore more bounds. An exsample Palmitoleic acid.
• Room temperature is more liquide commonly.

Essential Fatty Acids

• Linoleic acid, from α-Linolenic acid, which leads back to Arachidonic Acid.
• Only from diet can you get thes molecules.

Triaclyglycerols(Triglycerades)

• Triaclyglycerols forms from triesters.
• Lipses hydrolyses the triglycerides with enzymes.

Derived Lipids

• Vitamin A Functions deficient is when nights is dark.
• Vitamin D Functions calcium metabolisms deficient on children called "Rickets"
• Vitamin E Functions as antioxidant.
• Vitamin K Functions deficient impaired Blood.

Prostaglandins

• Involved in inflammation, blood clotting, and immune response.
• Lipids that c from units "Terpenes"

Membrane transport

Diffusion is the flow done, with no require energy. Facilitated Diffuions dose not require energy either and molecules go through carriees, on the other hand, require energy to flow through the membrane.

Lipoproteins

• Transfer cholerterol or lipids with in the blood for transport.
• Not polar region is in the core and the other region faces outward.

Classifications

• Based on density with ultracentrifugation.
• They also based Apo protein.
  • A B is mostly by chylomicrons.

Functions Of Lipoproteins

• Transports lipids by the means for utilizing, sorting, or to remove.
• Activation through enzymes that facilitate through metabolic lipids.
• Lipase helps break down which facilitates lipopreteins.

Metabolism of Lipopreteins

Chylomicrons: Formed in intestinal mucosal cells, they transport dietary triglycerides and cholesterol. Lipoprotein Lipasehydrolyzes the molecule in capillary tissues, releasing free fatty acids for energy.

Endogenous Pathway

LDL rich in cholesterol is transported through cells with a LDL transfer.

• HDL Synthesized helps with transfers from the tissues and transfer to back for cholestrerol.

Lipopreteins & Their Functions

Apo aids LCAT and helps with backwards with transfer. Essential to the chylimicron formation

Disorders of Lipopreteins

Abo causes levels and there will be over production causes by APO and there will be VLDL.

Hereditary disorder

Genetic defects in Apo B synthesis can create absense with chylomicrons, which creates poor absortion.

Introduction to Biological Membranes, What Are Biological Membranes?

• Surround cells and have membranes
• Selectively have permeability, and act on cells interaction

Composition of Membranes

Carbohydrates act as Glycoproteins. Protein will make and act on membranes. Lipids will support and act a backbone.

Membrane Structure

Lipids will be bilayers and have phospholipids and are ampiophatic this mean they repulse and interact with water.

Fluidity of Membrane

• Saturated can reduce a fluidity.
• Membrane assymetry.
• Assymetric and different, Phosphatidylserine and phosphatidylethanolamine

Types of membrane, Integral Membrane Proteins.

Membrane proteins are embedded but never cross, integral ones often span through it. Transports which help proteins facilitate.

Peheriperal membrane Proteins.

Are just atatched but are not embedded, they interact through others of the structure and non covalent.

Functions Of the membranes.

Membranes help proteins and moleculs to leave and enter cells.

Enzymatic Activity

Proteins in the membrane can behave and act on cells.

Transduction signals.

They can act as signals known as the harmones.

Cell-Cell Recognition

Can be identified through glycoproteins in the cells.

Enter Cellular joining.

Facilitate communication by maintain structers through the tissues

Attachment to the Cytoskelaton and extracellular matrix.

Supports and maintains shapes, to help protein be steady and to bind cell.

Types - Simple and Facilitated Diffussion

Molecules from down can transport through. - Requires energy not. - Requires transport protein to pass through.

Types, Active transport .

Transports from low to high require engery for moving the molecuels - Aqpaurines Water balance is regulated by Aqpaurines.

Endocytosis

Cells takes through molecules such has Phagocytosis and Endosytosis.

NULECATIDES .

Building block are nucleatides and acis.

Composed of .

• 3 main components: Sugar(5), Nitrogen base(1), And phosphate groups These are monomers for nucleic.

Structure of Nucleotides

These molecules contain nitroges, which lead to pyrimidines and purines. Purines Adenine and Guanine. Pyrimidines cytosine in timine. Also it contais a component called sugar that is derived from ribose.

Phospahte groups. Nucleosides vs . Nucleotides

Attached to 5 carbon to the sugar nucleosides. They also can vary ither be tri,monor or dinucleotid. Phosphae but dont contais a phosphates they are nucleosides.

Namming nucleotides

Specific bases , sugar and phostes are named under nucleutides.

Biosynthesis of nucleotides.

The precursors contain are synthesize by nucleutides.

Functions of Nucleotides

Forms and are united where they are essential for Dna replication. Atp is one of primary energy source. Also with codens that allow functions. Allow with synthases and transfering also with regulators.

Uptake Dietary

From 5% and its not so great to absorb nutrinters .

Synthesis

All the compounds and precursor with a good and all thins All of this process is essential for minimal nutriment.

Structures ,Properties, and Reactions of Amino Acids

There are 20 total encoded in DNA

• all are in 3 structures and the rest are know has selenopysteine
• all have abbrviation and code A is a good example. have Amino and carboxyl groups.

Chiral center.

19 / 20 Amino acids have this.

Amino acids are found in all cell

Also helps in monitoring preventitive aids.

Measurements of amino acid.

• Ninhidryn produces colors.
• Specific is more specific bacteria is
• Cromatography bases helps that allows affinity for a fraction.

Cromatorraphy.

Uses intercations it allows separation and it depends and some moleculses

• Collected as fractions and anaylsed

Clinicall Realted

• Menta lretardation is comon
• Is essential for all profile
• Tandenn is high speed because there are mutile metablise,

Introduction to Carbohydrrates

• O2 is from formula. Classify depend on size and carbon chain. The units the number of sugars. Sterocemisty.

Classifications

Disaccharides (2units) (e.g., sucrose, lactose, maltose. Monosaccharide (one unit) E.g( glucose, fructose and galactose)

Monosac

Fructose, Glacatose . Glucose. Cyclases in the monosac leads to isomers and can make chains. From glucose , galactose.

• Polysac Amylose. Glycogen also chains.
• Isomeros

Have the same the spatial that may vary. Mutartotation. Is for and which they are equilibiruium. Functions of Carbs

• Enerry main source : Storage and singnal.

Healt and implications

Excess Carbs : To get the body to become fat and storage it. Diets: Is important for a better life style.