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Week one: Anatomy and Physiology Notes

by: Olivia may

Week one: Anatomy and Physiology Notes ANPS 019

Marketplace > University of Vermont > ANPS 019 > Week one Anatomy and Physiology Notes
Olivia may
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Lecture 1 and 2 notes/ objectives guide
Human Anatomy and Physiology
Sean Flynn
Class Notes
anatomy, Physiology, Chemical Bonds, structure of water, enzymes catalyze reactions, organic molecules




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This 3 page Class Notes was uploaded by Olivia may on Thursday February 25, 2016. The Class Notes belongs to ANPS 019 at University of Vermont taught by Sean Flynn in Fall 2016. Since its upload, it has received 112 views.


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Date Created: 02/25/16
Lecture 1 objectives     1.Describe the different kinds of chemical bonds    Covalent ­ Bonding between 2 nonmetals; sharing of electrons creating bounding  Polar­ sharing electrons unequally  Nonpolar­ sharing electrons equally     Ionic­ Bonding between a metal and nonmetal: complete transfer of electrons resulting in two  charged atoms that are then attracted to each other  Cation­ + charged ion  Antion­ ­ charged ion    Hydrogen bonding­ because hydrogen is the smallest atom it usually has polar bonds which  results in a partial positive charge which allows for weak attraction to a negative ion    2.Explain the structure of water and how it works as a solvent     The structure of water is bent, which means it has a + pole and a ­ pole due to an unequal  sharing of electrons, water molecules are held together but easily broken electron bounds and  are attracted to any solute with charged atoms    3. Explain the relationship between pH and concentration of hydrogen ions in a solution  and relate this to the pH values of key body fluids    The lower the pH the higher the H+ concentration, more acidic   The higher the pH the lower the H+ concentration, more basic    Blood is relatively neutral mean there are = amounts of H+ and OH­ ions, stomach acid is very  acidic so there is a high [H+]    4. Describe the process which enzymes catalyze reactions    Reactants (substrates) interact to yield a product by binding to the active site of the enzyme to  form a temporary enzyme ­ substrate complex. The E­S substrate undergoes internal  reorganization that forms a product and is released.  Decreases activation energy, thus making a reaction more likely  Not used up in reaction  Very sensitive to temperature and pH change  ­Stability of the body allows for optimal reactions       Lecture 2 objectives    1. Explain why carbon is the core of Organic Molecules     Carbon has 4 valence electrons thus allowing it to from 4 bounds. Carbon can form single  bounds, double, and triple bounds.     2. Describe the basic structure of each of the four classes of Organic molecules, and  where they are used in the body    Lipids­​ mostly carbon and hydrogen, lack charges making them hydrophobic ­ not attracted to  water. 5 classes: P ​ hospholipids and Glycolipids­ ​  Cell membranes ​Fatty acids​­ energy storage  and building blocks ​Triglycerides ­ three fatty acids attached by dehydration synthesis to one  molec​ule of glycerol ​Glycerides­ ​  building blocks S​ teroids ​ cholesterol and sex hormones,  ​ corticosteroids ­ ​ egul​ te metabolism, important in lipid digestion, E ​ icosanoids­ ​  signaling  hormones ​Phospholipids ​polar on one end and non polar on the other Phosphorus (head),  glycerol backbone, 2 fatty acid chains (tail)      Carbohydrates­​ Typically have an ­H and an ­OH, “sugar group” important for energy, charged  > hydrophilic, monosaccharides 1 sugar molecules Disaccharides 2 or more sugar molecules,  Glycogen ­ the polysaccharides storage of glucose    Proteins­​ 20 Amino acids  (R)       (Carbon, amino group, carboxylic acid, and R group), used for support and movement.  enzymes have many functions (transportation, catalysis, pH, metab, body defense, and  protein management). Some charged, some hydrophilic some hydrophobic. acid and  amino group interact and form peptide bond (release of H2O).  primary:​ linear sequence of aminos  secondary​: helix sheet, beginning of interactions (alpha sheets: spiral, h bonds. beta  sheets: zigzags, pleated, h bonds)  Tertiary (globular):​ final shape, sensitive to pH and temp, globular form held together by  intermolecular bonds  quaternary: ​globular proteins meet, these proteins are only active when out together    Nucleic Acids​­ Made of Nucleotides containing Phosphate group (PO4), sugar group, nitrogen  containing base Types of Nitrogen bases: Purines ­ double ring molecules (adenine, guanine)  Pyrimidines­ single ring (cytosine, thymine, Uracil) Makes DNA ( Phsophate, suagr, base) and  RNA. Phosphate ends held together by  hydrogen bounds    3. Describe the structure of ATP and relate it to its ability to power chemical  reactions in the body    Made by adding a phosphate group to adenosine diphosphate (ADP­ Adenine, ribose, 2  phosphates) in a process called Phosphorylation. ATP (Adenine, ribose, 3 phosphates) is a high  energy compound, that energy can be released during ATP hydrolysis which is the removal of a  terminal phosphate group.  


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