Introduction Diabetes Bonding Biomolecules

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Introduction Diabetes Bonding Biomolecules
2015-03-02 03:17:36
Physiology Lecture
Lectures notes/ Test prep
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  1. What is Physiology?
    The study of organisms
  2. 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)
  3. What separates internal and external environments?
    • Epithelium 
    • -Ex Skin, lining of lungs, intestinal tract, and kidney tubules
  4. 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
  5. Total Body Water (TBW)
    • Volume of H20 in all the body's compartments 
    • Includes: Intracellular and Extracellular fluid
  6. Intracellular Fluid
    Fluid inside the cells
  7. Extracellular Fluid
    • Fluid outside the cells
    • Includes: Plasma and Interstitial Fluid
  8. Plasma vs interstitial fluid
    • Plasma: Liquid (non-cellular) portion of blood
    • Interstitial Fluid: Fluid (outside the blood) surrounding the cells
    • Both considered extracellular fluid
  9. Goal of physiology
    To maintain homeostasis
  10. Homeostasis
    • Maintenance of a relatively constant internal environment 
    • Unifying theme in physiology 
    • May be disrupted by disease
  11. 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
  12. Regulated variables of homeostasis
    • Temperature
    • pH
    • Salinity 
    • Dissolved gas concentration (02, CO2)
    • Nutrient and waste concentration
  13. What is a Set Point?
    Range for a regulated variable the body wants to maintain
  14. Blood Glucose Set point
    • 100mg/dl
    • Pancreas release insulin to maintain
  15. Set Point for Blood pH
    • 7.35 - 7.45
    • Lungs and kidneys help maintain
  16. 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
  17. Response after a change is detected
  18. Negative Feedback
    • Response moves the system in the opposite direction of initial change
    • Stabilizing 
    • More common
    • Ex: Body temp, blood glucose levels
  19. Positive Feedback
    • Response moves system in the same direction as the initial change 
    • Directional 
    • Less Common
    • Ex: Ovulation or child birth
  20. 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
  21. Four types of diabetes
    • Diabetes Mellitus I
    • Diabetes Mellitus II
    • Gestational Diabetes 
    • Diabetes Insipidus (rare)
  22. Diabetes Mellitus I
    • Inadequate insulin production 
    • Insulin dependent
  23. Diabetes Mellitus II
    • Body cells lose response to insulin 
    • NON-insulin dependent 
    • Most common
  24. Gestational Diabetes
    • Temp loss of sensitivity to insulin due to hormonal changes 
    • During pregnancy
  25. Diabetes Insipidus
    • Inadequate anit-diuretic hormone secretion
    • High Urine Volume 
    • Rare
  26. How does one develop diabetes?
    • Obesity: High body fat relative to lean body mass
    • Sedentary lifestyle
  27. Ionic Bonding
    • Electron is transfered from one element to another 
    • Electronegativity: One strong, one weak
    • Between two ions w/ opposite charges
    • Ex: NaCl
  28. Covalent Bonding
    • Electrons are shared 
    • Electronegativity: relatively equal 
    • Non polar: equal sharing (CH4)
    • Polar: unequal sharing (H20)
  29. Hydrogen Bonds
    • Opposite charges on adjacent molecules -> attraction
    • Slight + charges near H and - charges near O
    • Ex: Water molecules binding to each other
  30. What are biomolecules?
    • Molecules synthesized by cells 
    • Contain C-C covalent bonds
    • Often form rings or chain structures
  31. How do we make biomolecules?
    Dehydration synthesis: Forming covalent bonds by removal of water
  32. How do we breakdown biomolecules?
    Hydrolysis: Breaking covalent bonds with the addition of water
  33. 4 Types of biomolecules
    • Carbohydrates 
    • Lipids 
    • Proteins
    • Nucleic Acids
  34. Carbohydrates (Elements, Properties and 2 types)
    • Contain: C, H, O (C+H2O)
    • Properties: Polar -> Hydrophilic 
    • Types: Simple Sugars and Complex carbohydrates
  35. Simple sugars (function and types)
    • Funtion: Fast energy
    • Types: Monosaccharides- one sugar (ex-Glucose/Frutose), Disaccharide- 2 sugars (Sucrose, Lactose)
  36. 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)
  37. Lipids (Elements, Properties 4 types)
    • Contain: C, H, O
    • Properties: NON polar -> Hydrophobic 
    • Types: Triglycerides, Phospholipids (cell membrane, Eicosanoids, Sterols
  38. Triglycerides (Structure, Function, Types)
    • Structure: 1 Glycerol and 3 fatty acids
    • Function: Energy storage, insulation, protection
    • Types: Saturated fat and Unsaturated fat
  39. Saturated fat
    • Types of triglyceride 
    • Contains no double bonds
    • Tightly packed
    • Solid at room temp
  40. Unsaturated fat
    • Type of triglyceride 
    • Contain double bonds
    • Loosely Packed 
    • Liquid at room temp
  41. Phospholipids (Structure,Function)
    • Structure: 1 Glycerol, 1 polar phosphate group, and 2 non polar fatty acids
    • Function: Membrane structure
  42. Eicosanoids (Structure and Function)
    • Structure: Ring structure, 2 fatty acids 
    • Functions: Cellular communication
    • Ex: prostaglandin 
    • Resemble phospholipids
  43. 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
  44. What do elements do proteins contain?
    • Carbon
    • Hydrogen
    • Oxygen
    • Nitrogen
  45. 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
  46. 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
  47. 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
  48. Beat pleated sheets
    Pleats, amino acids is a organized wavey form
  49. 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)
  50. What elements do Nucleic acids contain
    • Carbon
    • Hydrogen 
    • Oxygen
    • Nitrogen
    • Phosphate

  51. Nucleic Acids (Properties, structure, function, types)
    • Properties: Polar -> Hydrophilic 
    • Structure: Chain of nucleotides 
    • Function: Stores genetic information (DNA)/DNA expression (RNA)
    • Types: DNA/RNA
  52. Nucleotide (components, Use, types)
    • Components: Phosphate group, Sugar, Nitrogenous base
    • Use: Complementary base pairing 
    • Types: Puriens (A+G), Pyrimidnes (C+T+U)
  53. 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
  54. DNA
    • Double stranded helix
    • Sugar - deoxyribose 
    • Thymine binds to Adenine
  55. RNA
    • Single stranded 
    • Sugar - Ribose
    • Uracil binds to Adenine 
    • 3 types: mRNA, tRNA, rRNA
  56. 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
  57. DNA replication
    • Located in nucleus 
    • Semi conservative 
    • works bidirectional
  58. 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 
  59. Protein synthesis
    • Central Dogma of Molecular biology 
    • DNA - (transcription)-> mRNA - (translation)-> Protein
  60. Transcription
    • DNA-> RNA
    • Location: Nucleus 
    • Enzymes: DNA Polymerase (Unwinds DNA and makes complementary RNA strand)
  61. Translation (Location, organelle)
    • mRNA -> Protein
    • Location: Cytoplasm
    • Organelle involved: Ribosome
  62. 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)
  63. Genetic code
    • mRNA language are codons (groups of 3 nucleic acids)
    • Sense (aa) nonsense (stop codons) 
    • 64 possible codons/ only 20 amino acids
  64. Start Codon
    AUG - methionine
  65. Stop Codon

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