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Notes physiology quiz notes quiz

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2022/2023

Uploaded on 01/26/2026

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Ch. 2
ELECTRON ROLES
1) Covalent Bonds strongest; e- shared between atoms make molecule; double, single, triple bond
2) Ions gain or lose e- to gain charges
CATIONS: Na+ K+ Ca+ H+ Mg+2 ANIONS: Cl- HCO3- HPO42- SO42-
3) High-Energy Electrons e- capture energy from environment to transfer to atom; energy carriers; NADH & FADH2
4) Free Radicals unstable; unpaired e-, highly reactive, breakdown bonds, neutralized by antioxidants (Vit. A,E,C); Cause: UV or smoke
CHEMICAL BONDS
1) Covalent Bonds atoms share e-
Nonpolar Molecules even distribution of e- ; lipid soluble; EX) Oil
Polar Molecules Regions of partial charge; positive and negative end; water soluble; EX) water
2) Non-covalent Bonds facilitate reversible binding of molecules
IONIC BONDS electrostatic attraction; atoms gain or lose e-, opposite charges attract
HYDROGEN BONDS Weak bond; between H atom and O, N, or F atom; Responsible for water surface tension
VAN DER WAALS FORCES weak nonspecific attractions of e-
NONCOVALENT INTERACTIONS
allow protein to associate reversible with other molecules, creating enzymes and substrates or signal receptors
Solubility ability to dissolve in a solvent
Hydrophilic soluble in water; polar or ionic molecules
Hydrophobic not soluble in water/lipid soluble; non polar molecules
Solution solute dissolved in solvent (water)
Concentration = solute amount / volume of solution
PROTEIN INTERACTIONS
1) Enzymes 4) Receptors 7) Regulatory Proteins
2) Membrane transporters 5) Binding proteins
3) Signal Molecules 6) Immunoglobulins
Ligand any molecule or ion that binds to another molecule
Substrates ligands that bind to enzymes and membrane transporters
Binding Site Active site; specifity, affinity, competition, saturation, molecular complimentarity
Affinity degree to which a protein is attached to a ligand
Law of Mass action concentration of reactant = to reaction; equilibrium constant
ESSENTIAL FOR BINDING ACTIVITY
1) COFACTORS required for ligand binding at site
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Ch. 2 ELECTRON ROLES

  1. Covalent Bonds strongest; e- shared between atoms make molecule; double, single, triple bond
  2. Ions gain or lose e- to gain charges CATIONS: Na+ K+ Ca+ H+ Mg+2 ANIONS: Cl- HCO3- HPO42- SO42-
  3. High-Energy Electrons e- capture energy from environment to transfer to atom; energy carriers; NADH & FADH
  4. Free Radicals unstable; unpaired e-, highly reactive, breakdown bonds, neutralized by antioxidants (Vit. A,E,C); Cause: UV or smoke CHEMICAL BONDS
  5. Covalent Bonds atoms share e- Nonpolar Molecules even distribution of e- ; lipid soluble; EX) Oil Polar Molecules Regions of partial charge; positive and negative end; water soluble; EX) water
  6. Non-covalent Bonds facilitate reversible binding of molecules IONIC BONDS electrostatic attraction; atoms gain or lose e-, opposite charges attract HYDROGEN BONDS Weak bond; between H atom and O, N, or F atom; Responsible for water surface tension VAN DER WAALS FORCES weak nonspecific attractions of e- NONCOVALENT INTERACTIONS allow protein to associate reversible with other molecules, creating enzymes and substrates or signal receptors Solubility ability to dissolve in a solvent Hydrophilic soluble in water; polar or ionic molecules Hydrophobic not soluble in water/lipid soluble; non polar molecules Solution solute dissolved in solvent (water) Concentration = solute amount / volume of solution PROTEIN INTERACTIONS
  7. Enzymes 4) Receptors 7) Regulatory Proteins
  8. Membrane transporters 5) Binding proteins
  9. Signal Molecules 6) Immunoglobulins Ligand any molecule or ion that binds to another molecule Substrates ligands that bind to enzymes and membrane transporters Binding Site Active site; specifity, affinity, competition, saturation, molecular complimentarity Affinity degree to which a protein is attached to a ligand Law of Mass action concentration of reactant = to reaction; equilibrium constant ESSENTIAL FOR BINDING ACTIVITY
  10. COFACTORS required for ligand binding at site

Dissociation

a

:it

te

Ud

  1. PROTEOLYTIC ACTIVATION converts inactive to active by removing part of molecules (digestive enzymes) MODULATORS AND FACTORS THAT ALTER BINDING OR ACTIVITY
  2. COMPETITIVE INHIBITOR competes directly at site with ligand by binding reversible to active site
  3. IRREVERSIBLE INHIBITOR binds to binding site and cant be displaced
  4. ALLOSTERIC MODULATOR binds to protein away from bidning site and changes activity; inhibit or activate
  5. COVALENT MODULATOR bond covalently to protein and change its activity
  6. pH and Temp alter 3-d shape by disrupting hydrogen or S-S bonds; irreversible if protein denatured (loses shape) CH. FUNCTIONAL COMPARTMENTS OF BODY MAJOR CAVITIES cranial, thoracic, abdominopelvic FLUID FILLED COMPARTMENTS circulatory system, eyes, Cerebrospinal fluid, pleura and pericardial sacs Lumen anterior of any hollow organ ; for some organs its an extension of external environment Hollow Organs heart, lungs, blood vessels, intestines BIOLOGICAL MEMBRANES Cell Membrane Physical Isolation, Regulate exchange with env, communication with cell and env, Structural support, & Secretion Integral Proteins tightly bound to membrane; only removed by disrupting membrane structure Peripheral proteins can be removed without disrupting membrane integrity Transmembrane proteins cross lipid bilayer Cholesterol inserts itself into lipid layer; allows membrane to be flexible Glycocalyx mark proteins; sugar INTRACELLULAR COMPARTMENTS Differentiation selected genes are active to lead to specialized cell Cytoplasm Cytosol intracellular fluid Inclusion area in direct contact with cytosol; lack membranes Ribosomes manufacture proteins (fixed RER vs free) Membranous Organelles Mitochondria ATP synthesis; has own DNA purely from mom Endoplasmic Reticulum RER = protein synthesis SER = synthesizes lipid, stores Ca, Detox Golgi Apparatus protein packaging Lysozomes digestive enzymes; storage vesicles Peroxisomes enzymes break fatty acids
  1. MUSCLE TISSUE contractile (make force and movement) and generate electrical signals Types Cardiac, Smooth, Skeletal
  2. NEURAL TISSUE Neurons (nerve cells) and Neuroglia (glial cells) TISSUE REMODELING Necrosis cell death from injury; inflammation; hypoxia most common Apopotosis programmed cell death or suicide; menopause Stem Cells Cell Replacement thru mitosis but retain ability to divide; high plasticity; nonspecialized; in red bone marrow CH. PROPERTIES OF LIVING ORGANISMS
  3. Cell is the Basic unit of Organization
  4. Metabolism = acquire, transform, store and use every
  5. Sense and respond to internal and external environments
  6. Maintain Homeostaiss
  7. Store DNA/Information
  8. Reproduce/Grow
  9. Have emergent properties that cant be predicted from sum of all parts
  10. Individuals adapt and species evolve ENERGY Heliotropic oraganisms depend on sun for energy Energy capacity to do work Chemical work making and breaking chemical bonds Transport Work moving ions, molecules, and large particles; concentration gradients Mechanical Work moving organelles, changing cell shape, beating flagella and cilia, and contracting muscles (gross movements) Kinetic Energy energy of motion Potential energy stored Energy Transformation Efficiency energy can be converted from one form to another Thermodynamics study of energy use 1st law of Thermodynamics law of conservation of energy; total amount of energy in universe is constant 2nd Law of Thermodynamics processes move from state of order to disorder (entropy); Ex) loss of energy Bioenergetics study of energy flow thru biogical systems Chemical Reaction Reactants becomes products; Reaction Rate (speed of reaction) Free energy potential energy stored in chemical bonds of a molecule; readily available for reactions to happen Activation Energy initial input of energy needed to make reactants react with each other

energy Free Energy change of reaction means the reaction either released or trapped energy Exergonic Reaction free energy of product lower than free energy of reactants; energy releasing Endergonic Reaction products retain part of activation energy making free energy of products more; energy utlizing/trapping Net free Energy Change determines reaction reversible vs irreversible Enzymes proteins; speed up rate of chemical reaction; Catalysts (enzyme molecules dont change); lower activation Substrates the reactants Proenzymes/Zymogens inactive enzymes and need proteolytic activation; initial enzymes produced Coenzymes cofactors acting enzymes; Ex) Vitamins Metabolism all chemical reactions in an organism Catabolism exergonic; energy releasing; breakdown large to small molecules Anabolism Endergonic; energy utilizing; synthesize large molecules from small molecules Kilocalories energy released from or stored in chemical bonds; amount of energy to raise temp of 1L of H2O by 1C HOW CELLS REGULATE METABOLIC PATHWAYS? controlling enzyme concentration, producing modulators, using different enzymes, compartmentalizing enzymes, maintaining ATP and ADP ratio ATP transfers energy between reactions; high energy phosphate group Aerobic metabolism need oxygen; 1 glucose = 30-32 ATP Anaerobic Metabolism No Oxygen; 1 glucose = 2 ATP & 2 Lactate Catabolic Pathways 1) Glycolysis 2) Citric Acid Cycle 3) Electron Transport System Glycolysis Citric Acid Cycle LOCATION: Cytosol LOCATION: Mitochondrial Matrix REACTANT: Glucose REACTANT: Acetyl-CoA PRODUCTS: 2 Pyruvate & 2 Net ATPS PRODUCTS: High energy e-, FADH2, NADH, CO OXYGEN: No OXYGEN: Yes Electron Transport System LOCATION: inter membrane space of mitochondria REACTANT: NADH, FADH PRODUCT: ATP, H2O OXYGEN: Yes, last e- acceptor Cytochrome enzymes remove protein from NADH and FADH