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What is Physiology?
The study of organisms
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External vs Internal environment
- External environment are components OUTSIDE the body (air, nutrients, H20, inorganic cmpds)
- Internal environment are components INSIDE the body (Cells, fluids)
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What separates internal and external environments?
- Epithelium
- -Ex Skin, lining of lungs, intestinal tract, and kidney tubules
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The Human body requires contact with external environment. What are the problems and solutions for this?
- Problem: Not all cells are in direct contact with external environment
- Solution: Fluid compartments allow for cell communication
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Total Body Water (TBW)
- Volume of H20 in all the body's compartments
- Includes: Intracellular and Extracellular fluid
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Intracellular Fluid
Fluid inside the cells
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Extracellular Fluid
- Fluid outside the cells
- Includes: Plasma and Interstitial Fluid
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Plasma vs interstitial fluid
- Plasma: Liquid (non-cellular) portion of blood
- Interstitial Fluid: Fluid (outside the blood) surrounding the cells
- Both considered extracellular fluid
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Goal of physiology
To maintain homeostasis
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Homeostasis
- Maintenance of a relatively constant internal environment
- Unifying theme in physiology
- May be disrupted by disease
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Two types of Homeostatic control systems and how they work
- Intrinsic/ Local control: Inherent in an organ
- Extrinsic/ Systemic control: Regulatory mechanism initiated outside organ, Endocrine & Nervous system, Coordinated response from several different organs
- Both goals are homeostasis
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Regulated variables of homeostasis
- Temperature
- pH
- Salinity
- Dissolved gas concentration (02, CO2)
- Nutrient and waste concentration
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What is a Set Point?
Range for a regulated variable the body wants to maintain
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Blood Glucose Set point
- 100mg/dl
- Pancreas release insulin to maintain
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Set Point for Blood pH
- 7.35 - 7.45
- Lungs and kidneys help maintain
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Homeostatic response to out of range set points
- 1. Stimulus: Change from set point (Error Signal)
- 2. Sensor: Detects stimulus (sensor & Beta cells)
- 3. Integrating center: Receives input from receptors(Beat cells), Determines needed outputs to effectors
- 4. Effectors: Receives output to response to stimulus
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Response after a change is detected
Feedback
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Negative Feedback
- Response moves the system in the opposite direction of initial change
- Stabilizing
- More common
- Ex: Body temp, blood glucose levels
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Positive Feedback
- Response moves system in the same direction as the initial change
- Directional
- Less Common
- Ex: Ovulation or child birth
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What is Diabetes? What does it affect?
- Metabolic disease affecting: Blood glucose levels and high urine volume
- Results: Excessive thirst, Excessive fluid loss, Eventually all body systems are affected
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Four types of diabetes
- Diabetes Mellitus I
- Diabetes Mellitus II
- Gestational Diabetes
- Diabetes Insipidus (rare)
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Diabetes Mellitus I
- Inadequate insulin production
- Insulin dependent
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Diabetes Mellitus II
- Body cells lose response to insulin
- NON-insulin dependent
- Most common
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Gestational Diabetes
- Temp loss of sensitivity to insulin due to hormonal changes
- During pregnancy
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Diabetes Insipidus
- Inadequate anit-diuretic hormone secretion
- High Urine Volume
- Rare
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How does one develop diabetes?
- Obesity: High body fat relative to lean body mass
- Sedentary lifestyle
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Ionic Bonding
- Electron is transfered from one element to another
- Electronegativity: One strong, one weak
- Between two ions w/ opposite charges
- Ex: NaCl
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Covalent Bonding
- Electrons are shared
- Electronegativity: relatively equal
- Non polar: equal sharing (CH4)
- Polar: unequal sharing (H20)
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Hydrogen Bonds
- Opposite charges on adjacent molecules -> attraction
- Slight + charges near H and - charges near O
- Ex: Water molecules binding to each other
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What are biomolecules?
- Molecules synthesized by cells
- Contain C-C covalent bonds
- Often form rings or chain structures
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How do we make biomolecules?
Dehydration synthesis: Forming covalent bonds by removal of water
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How do we breakdown biomolecules?
Hydrolysis: Breaking covalent bonds with the addition of water
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4 Types of biomolecules
- Carbohydrates
- Lipids
- Proteins
- Nucleic Acids
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Carbohydrates (Elements, Properties and 2 types)
- Contain: C, H, O (C+H2O)
- Properties: Polar -> Hydrophilic
- Types: Simple Sugars and Complex carbohydrates
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Simple sugars (function and types)
- Funtion: Fast energy
- Types: Monosaccharides- one sugar (ex-Glucose/Frutose), Disaccharide- 2 sugars (Sucrose, Lactose)
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Complex Carbohydrates (Function and Types)
- Function: Energy storage or structural support in plants. Component of cell membrane
- Types: Polysaccharide- Chain of sugars (ex glycogen, starch, cellulose, chitin, rice potatoes)
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Lipids (Elements, Properties 4 types)
- Contain: C, H, O
- Properties: NON polar -> Hydrophobic
- Types: Triglycerides, Phospholipids (cell membrane, Eicosanoids, Sterols
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Triglycerides (Structure, Function, Types)
- Structure: 1 Glycerol and 3 fatty acids
- Function: Energy storage, insulation, protection
- Types: Saturated fat and Unsaturated fat
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Saturated fat
- Types of triglyceride
- Contains no double bonds
- Tightly packed
- Solid at room temp
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Unsaturated fat
- Type of triglyceride
- Contain double bonds
- Loosely Packed
- Liquid at room temp
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Phospholipids (Structure,Function)
- Structure: 1 Glycerol, 1 polar phosphate group, and 2 non polar fatty acids
- Function: Membrane structure
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Eicosanoids (Structure and Function)
- Structure: Ring structure, 2 fatty acids
- Functions: Cellular communication
- Ex: prostaglandin
- Resemble phospholipids
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Sterols (structure and function)
- Structure: 4 carbon rings with side chains (3 diamonds and a house)
- Function: Membrane fluidity (helps maintain integrity), Cellular communication, others
- Ex: Cholesterol, testosterone, Vitamin D
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What do elements do proteins contain?
- Carbon
- Hydrogen
- Oxygen
- Nitrogen
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Protein Structure and Function
- Structure: Chain of amino acids (polypeptide ~20 AAs)/ Folded 0-0-0- -> sasda
- Function: Structure support, enzymatic activity, Chemical messengers, Receptors
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Amino Acids (Structre and structure levels)
- Structure: Central Carbon, Amine group (NH2), Carboxyl group (COOH), and R group which determines type of protein.
- Levels:Primary, Secondary, Tertiary, Quanternary
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Primary and Secondary Structures
- In Amino Acids
- Primary: Sequence of Amino acids (peptide bonds)
- Secondary: Structural Motifs (H-bonds) like Alpha Helix or beta pleated sheets
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Beat pleated sheets
Pleats, amino acids is a organized wavey form
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Tertiary vs Quaternary Structures
- In amino acids
- Tertiary: Large scare motifs formed by interactions between R groups (H, Ionic, disulfide bonds)
- Quaternary: Bonding w/ multiple polypeptide chains (all types of bondingm hemoglobin)
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What elements do Nucleic acids contain
- Carbon
- Hydrogen
- Oxygen
- Nitrogen
- Phosphate
(HOPCH)
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Nucleic Acids (Properties, structure, function, types)
- Properties: Polar -> Hydrophilic
- Structure: Chain of nucleotides
- Function: Stores genetic information (DNA)/DNA expression (RNA)
- Types: DNA/RNA
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Nucleotide (components, Use, types)
- Components: Phosphate group, Sugar, Nitrogenous base
- Use: Complementary base pairing
- Types: Puriens (A+G), Pyrimidnes (C+T+U)
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List all types of nitrogenous bases and their pairs
- Adenine, Guanine, Cytosine, Thymine in DNA, or Uracil in RNA
- A-T (DNA)
- A-U (RNA)
- G-C
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DNA
- Double stranded helix
- Sugar - deoxyribose
- Thymine binds to Adenine
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RNA
- Single stranded
- Sugar - Ribose
- Uracil binds to Adenine
- 3 types: mRNA, tRNA, rRNA
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Types of RNA and functions
- mRNA: Messenger RNA, Nucleus -> Ribosome in cytoplasm
- tRNA: Transfer RNA, important to protein synthesis
- rRNA: Ribosomal RNA, part of the ribosome
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DNA replication
- Located in nucleus
- Semi conservative
- works bidirectional
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Enzymes involved in DNA replication
- Helicase: Unwinds double helix
- DNA Polyamerase: Adds nucleotides to each unwound strand (51->31)
- Leading strand: DNA polyamerase adds as unwinding occurs
- Lagging strand: Polyamerase adds 5-3 must back track aka okazami fragments
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Protein synthesis
- Central Dogma of Molecular biology
- DNA - (transcription)-> mRNA - (translation)-> Protein
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Transcription
- DNA-> RNA
- Location: Nucleus
- Enzymes: DNA Polymerase (Unwinds DNA and makes complementary RNA strand)
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Translation (Location, organelle)
- mRNA -> Protein
- Location: Cytoplasm
- Organelle involved: Ribosome
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Process of Translation
- mRNA becomes associated with a ribosome
- Start codon is exposed and tRNA w/ complementary anticodon binds
- Next codon of mRNA is exposed and tRNA binds
- Peptide bonds form between two amino acids
- Ribosome moves along mRNA to expose other codon (Repeat until stop codon)
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Genetic code
- mRNA language are codons (groups of 3 nucleic acids)
- Sense (aa) nonsense (stop codons)
- 64 possible codons/ only 20 amino acids
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Start Codon
AUG - methionine
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