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General Biology 115 Final Exam/316 Questions with Solutions
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General Biology 115 Final Exam/316 Questions with Solutions
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General Biology 115 FinalExam/316 Questions with
Solutions
How does long term memory work? - -Activated when needed => pulled into
short term (working) memory
-Long term potentiation - -use of information is like a sorting process
-T/F: If information is not used, then it is discarded - -True
-LTP is facillitated by - -Chunking
-Emeregnce - -The whole is greater than the sum of the parts
-Emergent Properties - -Results from the arrangement and interaction of
parts within a system
-Reductionism - -Reduction of complex systems to simpler components that
are more manageable to study
-Scientific Method - -Make an observation
Do background research
Make a hypothesis
Create an experiment
Evaluate the results of the experiment
If the predictions are wrong, make a new hypothesis and start over from step
3
Revise predictions
Repeat and verify
-4 most abundant elements - -C, H, O, N
-Ionic bonds - -Between atoms => the more electronegative elements
steals an electron
-Van der Waals Interactions - --Develop because electrons are in constant
motion
-single interaction is weak but multiple are strong
-Hydrogen bonds - --very strong dipole-dipole interaction
-H + F, O, N
, -Cohesive behavior - --polar molecules side with different charges are
attracted to each other
-surface tension is a measure of how hard it is to break the surface of a liquid
-Hydrophillic - -Ions, salts, polar, "water loving"
-Hydrophobic - -Lipids, nonpolar, "water hating"
-Organic compounds - --carbon based compounds
-carbon bonded to another carbon or hydrogen
-Hydrocarbons - --only hydrogen and carbon
-nonpolar, uncharged, hydrophobic
-Hydroxyl group - --alcohol
-polar
-form hydrogen bodns with water
-hydrophillic
-Ketone - --internal carbonyl group
-polar
-hydrophillic
-Aldehyde - --terminal carbonyl group
-polar
-hydrophillic
-Carboxyl group - --polar
-hydrophillic
-very acidic
-Amino group - --proton acceptor => basic
-hydrophillic
-Sulfhydryl group - --structure of some proteins
-less polar than a hydroxyl group
-Phosphate group - --contributes a negative charge
-acidic
-hydrophillic
-phospholipids & nucleic acids
-Methyl group - --nonpolar hydrocarbon
-hydrophobic
-control of gene expression
-shape and function of sex hormones
, -Macromolecules - --large complex molecules that are formed by thousands
of atoms
-carbohydrates, lipids, proteins, nucleic acids
-Enzymes - -speed up chemical reactions
-Hydrolysis - --"to break with water"
-using water to break polymers
-regulated by hydrolyses
-Dehyration synthesis - --synthesizes monomers together
-removes water
regulated by dehydrogenase
-Carbohydrates - --fuel & building material
-hydrophillic
-polysaccharides attached to proteins = glycoproteins or lipids
-cell identification (ex: blood types)
-Lipids - --not true polymers
-hydrophobic
-dissolve in nonpolar solvents => nonpolar
-3 important families: fats, phospholipids, steroids
-Fats - --highly concentrated energy
-consists of one glycerol (3 carbon alcohol with 3 -OH) & 1-3 fatty acids
-Fatty Acids - --carboxyl group with a long, unbraided hydrocarbon tail
-added to glycerol during dehydration synthesis
-form a covalent bond => ester linkage
-triglyceride = main storage of fat
-Phospholipids - --glycerol & 2 fatty acids (hydrophobic)
-phosphate group (hydrophillic
-polar
-acidic
-Steroids - --3 rings with 6 carbons & 1 ring with 5 carbons
-differ in side chains or functional groups attached
-Proteins - --made of amino acids
-monomers are bound together with peptide bonds through dehydration
synthesis => becomes polypeptide
-primary structure => secondary structure => tertiary structure =>
quatinary structure
, -Primary structure of proteins - -sequence of amino acids joined by peptide
bonds in a polypeptide chain
-Secondary structure of proteins - --hydrogen bonds
-R groups do NOT participate
-alpha helix = coil
-beta pleated sheet
-Tertiary structure of proteins - --interrelationships of R groups fold into
particular 3D shapes
-can have all types of bonds (hydrogen, ionic, covalent, disulfide)
-Quatinary structure of proteins - --two or more polypeptide chains
-no more folding
-Denaturation - --a loss of a protein's native structure
-biologically inactive
-pH, salt concentration & temperature are all factors that can cause
denaturation
-low temperature slows down an enzymatic reaction
-even a short exposure to a high temperature can denature a protein
-Nucleic acids - --monomers are nucleotides
-transmit hereditary information & determine protein production
-4 factors of abiotic synthesis - -1) little / no free oxygen
2) source of energy
3) presence of chemical building blocks
4) time
-Miller & Urey experiment - --simulated early conditions of early Earth
-formed amino acids & other organic molecules
-Iron-Sulfur World Hypothesis - --life formed at the cracks of the ocean floor
=> hydrothermal vents
-hot water, carbon monoxide, and mineral such as iron & nickel sulfide
released
-Steps of abiogenesis - -1) abiotic synthesis of monomers
2) synthesis of macromolecules
3) formation of protocells
4) self-replicating DNA
-Synthesis of macromolecules - --formation of polymers from monomers
-monomers polymerize on hot sand or on rock
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