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Bio Principles II

QuestionAnswer
polar molecule charges are unevenly distributed
covalent bond sharing electrons
hydrogen bonds partial positive attracts partial negative, constantly break and reform
1st Property of Water: cohesion and adhesion of water cohesion: water molecules sticking together thru H Bonds adhesion: attraction btwn different substances
2nd Property of Water: moderation of temperature kinetic E, thermal E, temperature, heat
kilo 1,000
calorie amount of heat needed to raise the temp of 1g of water by 1 C
joule another unit of energy
specific heat amount of energy needed to be lost or gained to change temp by 1 C
H20 has high specific heat- due to H bonds absorb heat when H bonds break release heat when H bonds form
3rd Property of Water: Heat Absorption/ Evaporative Cooling absorb heat from hot air- cooling the air heat of vaporization- amount of heat absrobed when changed from liquid to gas evaporative cooling- vaporization pulls heat from the surface to drop temp.
4th Property of Water Ice floats H bonds in ice are more structured and longer than in liquid density decreases
Water is the solvent of life solution- liquid that a homogenous mixture solvent- dissolving agent solute- dissolved substance
hydration shell water surrounding solutes in a strucutred way
hydrophilic water loving- carbs, nucleic acids, globular proteins
hydrophobic water fearing- lipids, oils, transmembrane proteins
Acidic/ Basic H20 can transfer H between molecules
Acids easily donate/ release H- increase concentration of H in solution high pH
Bases easily accept H- decrease concentration of H in solution low pH
A pH of 7 is neutral
Buffers chemicals that help maintain specific pH, carbonic acid and bicarbonate
macromolecules carbohydrates, lipids, nucleic acids, and protein
enzymes specialized macromolecules that act as catalysts for a chemical reaction
Synthesis link monomers- dehydration reaction, requires E
Degraduation remove monomer from a polymer- hydrolysis reaction, doesn't require E
Carbohydrates sugars, monosacchrides, have a lot of carboxol groups, making them hydrophilic, use E, dehydration to link 2 monosacchrides into polysacchride- starch, glycogen, celluose
Starch polymer of alpha glucose linked by a 1.4 glycosidic bond, structure for plants
2 forms of starch amylose- straight and unbranched amylopectin- somewhat branched once about 30 will and 1.6 glycosidic bond to form branch
Glycogen polymer of alpha glucose with primarily 1.4 glycosidic and 1.6 glycosidic bonds which are highly branched and have about 10 sugars, provide energy storage in animals
Cellulose polymer of beta glucose with 1.4 glycosidic bonds, provide structure of cell walls for plants and algae
Lipids hydrophobic, made of hydrocarbons, energy storage
Fats Triglycerides- consists of two smaller molecules
Glycerol 3c alcohol
Fatty Acids carboxyl group
Types of Fatty Acids Saturated and Unsaturated
Saturated Fatty Acids max number of C-H bonds, no double, solid at room temp, used for animal fats, high melting temp
Unsaturated Fatty Acids 1 or more double bonds between, liquid at room temp, plants and fish, low melting temp
Phospholipids glycerol, 2 fatty acids, phosphate, hydrophilic head, hydrophobic tails, main function to from membranes
Steroids carbon skeleton with 4-fused rings, hydrophobic and cross membranes, function is hormone signalling, cholestrol
Cholestrol components of animal membranes, used to make hormones
Proteins are not for..... making energy
Functions of Protein enzymatic, defensive, storage, transport, hormonal, receptor, contractile and motor, and structure
Proteins are made up of amino acids, 20
What are the different groups in a protein chain? amino group, carboxyl group, R group
Protein Structure 3D shape of the protein
structure= function
1st layer of protein structure: primary sequence of amino acids, N terminus- C terminus
2nd layer of protein structure: secondary coils and folds alpha helix: coil- H bond between every 4th amino acid beta sheets: long chains that H bond
3rd layer of protein structure: tertiary 3D shape of 1 peptide, relies on non-covalent interactions due to side chains (R)
Noncovalent interactions ionic bonds, hydrophilic/phobic, H bonds
4th layer of protein structure: quartenary multiple peptides interacting
Created by: user-2021040
 

 



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