General Biology 115 Final Exam

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316 Terms

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How does long term memory work?

Activated when needed => pulled into short term (working) memory

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Long term potentiation

use of information is like a sorting process

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T/F: If information is not used, then it is discarded

True

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LTP is facillitated by

Chunking

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Emeregnce

The whole is greater than the sum of the parts

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Emergent Properties

Results from the arrangement and interaction of parts within a system

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Reductionism

Reduction of complex systems to simpler components that are more manageable to study

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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

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4 most abundant elements

C, H, O, N

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Ionic bonds

Between atoms => the more electronegative elements steals an electron

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Van der Waals Interactions

-Develop because electrons are in constant motion

-single interaction is weak but multiple are strong

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Hydrogen bonds

-very strong dipole-dipole interaction

-H + F, O, N

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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

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Hydrophillic

Ions, salts, polar, "water loving"

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Hydrophobic

Lipids, nonpolar, "water hating"

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Organic compounds

-carbon based compounds

-carbon bonded to another carbon or hydrogen

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Hydrocarbons

-only hydrogen and carbon

-nonpolar, uncharged, hydrophobic

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Hydroxyl group

-alcohol

-polar

-form hydrogen bodns with water

-hydrophillic

<p>-alcohol</p><p>-polar</p><p>-form hydrogen bodns with water</p><p>-hydrophillic</p>
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Ketone

-internal carbonyl group

-polar

-hydrophillic

<p>-internal carbonyl group</p><p>-polar</p><p>-hydrophillic</p>
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Aldehyde

-terminal carbonyl group

-polar

-hydrophillic

<p>-terminal carbonyl group</p><p>-polar</p><p>-hydrophillic</p>
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Carboxyl group

-polar

-hydrophillic

-very acidic

<p>-polar</p><p>-hydrophillic</p><p>-very acidic</p>
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Amino group

-proton acceptor => basic

-hydrophillic

<p>-proton acceptor =&gt; basic</p><p>-hydrophillic</p>
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Sulfhydryl group

-structure of some proteins

-less polar than a hydroxyl group

<p>-structure of some proteins</p><p>-less polar than a hydroxyl group</p>
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Phosphate group

-contributes a negative charge

-acidic

-hydrophillic

-phospholipids & nucleic acids

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Methyl group

-nonpolar hydrocarbon

-hydrophobic

-control of gene expression

-shape and function of sex hormones

<p>-nonpolar hydrocarbon</p><p>-hydrophobic</p><p>-control of gene expression</p><p>-shape and function of sex hormones</p>
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Macromolecules

-large complex molecules that are formed by thousands of atoms

-carbohydrates, lipids, proteins, nucleic acids

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Enzymes

speed up chemical reactions

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Hydrolysis

-"to break with water"

-using water to break polymers

-regulated by hydrolyses

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Dehyration synthesis

-synthesizes monomers together

-removes water

regulated by dehydrogenase

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Carbohydrates

-fuel & building material

-hydrophillic

-polysaccharides attached to proteins = glycoproteins or lipids

-cell identification (ex: blood types)

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Lipids

-not true polymers

-hydrophobic

-dissolve in nonpolar solvents => nonpolar

-3 important families: fats, phospholipids, steroids

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Fats

-highly concentrated energy

-consists of one glycerol (3 carbon alcohol with 3 -OH) & 1-3 fatty acids

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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

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Phospholipids

-glycerol & 2 fatty acids (hydrophobic)

-phosphate group (hydrophillic

-polar

-acidic

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Steroids

-3 rings with 6 carbons & 1 ring with 5 carbons

-differ in side chains or functional groups attached

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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

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Primary structure of proteins

sequence of amino acids joined by peptide bonds in a polypeptide chain

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Secondary structure of proteins

-hydrogen bonds

-R groups do NOT participate

-alpha helix = coil

-beta pleated sheet

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Tertiary structure of proteins

-interrelationships of R groups fold into particular 3D shapes

-can have all types of bonds (hydrogen, ionic, covalent, disulfide)

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Quatinary structure of proteins

-two or more polypeptide chains

-no more folding

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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

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Nucleic acids

-monomers are nucleotides

-transmit hereditary information & determine protein production

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4 factors of abiotic synthesis

1) little / no free oxygen

2) source of energy

3) presence of chemical building blocks

4) time

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Miller & Urey experiment

-simulated early conditions of early Earth

-formed amino acids & other organic molecules

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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

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Steps of abiogenesis

1) abiotic synthesis of monomers

2) synthesis of macromolecules

3) formation of protocells

4) self-replicating DNA

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Synthesis of macromolecules

-formation of polymers from monomers

-monomers polymerize on hot sand or on rock

-negative ions bind monomers

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Formation of protocells

-in water, lipids and other organic molecules spontaneously form vesicles

-organic polymers exhibit attributes of living cells (osmosis, homeostasis, division)

-no mechanism of heredity

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Self-replicating DNA

-RNA first nucleic acid in protocells

-RNA is capable of replicating itself & catalyzing protein synthesis: ribozymes

-DNA evolved later (double-stranded, more stable)

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Order of geologic time

Eons => Eras => Periods => Epochs

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Stromatolites

ancient bacterial mats on sedimentary layers

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Order that life was formed in

Prokaryotes => Photosynthetic Autotrophs => Aerobes

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Endosymbiotic theory

-mitochondria and plastids were initially small prokaryotes

-now are organelles of eukaryotic cells

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Cambrian explosion

-535~525 million years ago

-fossils appear to resemble modern animals

-rapid evolution => new animal body plans

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Cell theory states that

-all organisms are made up of cells

-all cells have 4 common features and a common evolutionary ancestor

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Light microscope

-can see things the size of about 2um

-stains or dyes increase contrast

-you can see nucleus but not smaller organelles

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Scanning electron microscope

electrons bounce off the outside of the object

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Transmission electron microscope

-electrons go all the way through the object

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Why aren't electron microscopes used all the time?

-cells must be killed (sliced / covered in gold)

-may alter their structure

-expensive

-tedious preparation

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Features of all cells

-plasma membrane: phospholipids

-cytosol: semifluid substance

-chromosomes: carry genes and make DNA

-ribosomes: make proteins & RNA

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Prokaryotic cells

-NO nucleus (there is a nucleoid form => DNA in an unbound region)

-NO organelles but have flagella, plasma membrane, fimbriae & cell wall

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Eukaryotic cells

-DNA in nucleus

-membrane bound organelles

-10x the size of prokaryotic cells

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Why are cells so small?

-plasma membrane acts as a selective barrier

-surface area to volume ratio (the bigger it is, the more places there are for things to enter / leave the cell)

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Endosymbiosis

-both mitochondria and chloroplasts once were prokaryotes

-both mitochondria and chloroplasts have inner membranes, enzymes, their own DNA, their own ribosomes, undergo binary fission and are small

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Nucleus

-DNA is organized in chromosomes

-DNA & proteins = chromatin

-RNA is the only thing that leaves the nucleus

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Nucleolus

-RNA & proteins

-No membrane

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Nuclear envelope

-made of 2 membranes => both are bilipid bilayers

-nuclear pores regulare entry & exit of the molecules

-is lined by nuclear lamina, which is composed of proteins & maintains the shape of the nucleus

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Ribosomes

-site of protein synthesis

-not membrane bound => ribosomes are not considered organelles

-free ribosomes => float around in the cytoplasm (both prokaryotes and eukaryotes)

-bound ribosomes are bound on the endoplasmic regulation (only eukaryotes)

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Endomembrane system

-made of a lipid bilayer

-separates internal contents from external environment & separates cell into many compartments

-function is to regulate protein traffic & performs metabolic functions in cell

-consists of: nuclear envelope, plasma membrane, endoplasmic reticulum, Golgi apparatus, lysosomes & vacuoles

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Plasma Membrane

-encloses cell contents

-controls material that goes in & comes out of cell

-selectively permeable

-no cell wall

-phospholipid bilayer

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Endoplasmic reticulum

-continuous with nuclear envelope

-smooth ER has no ribosomes & rough ER has ribosomes

-lumen = internal space

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Functions of the Rough Endoplasmic Reticulum

-has bound ribosomes => makes proteins

-proteins are folded and modified

-secrete glycoproteins (proteins that are covalently bonded to carbohydrates)

-distributes transport vesicles

-is a membrane factory for the cell

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Functions of the Smooth Endoplasmic Reticulum

-synthesize lipids

-metabolizes carbohydrates to break down glycogen and regulate blood glucose

-detoxifies drugs and poisons

-stores calcium ions

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Golgi Apparatus

-cis face is the receiving side of the endoplasmic reticulum

-trans face is the shipping side

-modifies products of the endoplasmic reticulum

-manufactures certain macromolecules

-sorta & packages materials into transport vesicles

-shipping product out of Golgi apparatus using vesicles

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Lysosomes

-digestive components

-sacs of hydrolytic or digestive enzymes

-primary lysosomes: buds off Golgi

-secondary lysosomes: primary lysosome fused with another structure

-breaks down complex molecules

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Vacuoles

-diverse maintenance compartments

-food vacuoles are formed by phagocytosis

-contractile vacuole: plant cells, organic compounds & water

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Membrane Proteins

-tend to be amphipathic

-integral or peripheral

-can move but can't be flipped

-hydrophobic => fold inside the protein

-hydrophilic => fold outside the protein

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Functions of Membrane Proteins

-transport

-enzymatic activity

-signal transduction

-cell cell recognition

-intercellular joining

-attachment to the cytoskeleton & extracellular matrix

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Fluid Mosaic Model

-membrane components can move laterally within one layer of the membrane

-fluidity depends on temperature, chain length / bends in tail, saturation, and amount of cholesterol

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Passive Transport

-doesn't use ATP

-moves with the gradient

-spontaneous

-results in dynamic equilibrium

-cells prefer passive transport

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Diffusion

-tendency for molecules of a substance to fill available space

-small gases like oxygen gas, carbon dioxide and nitrogen gas can pass through

-small nonpolar molecules like hydrocarbons can pass through

-small polar uncharged molecules like water can pass through

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Osmosis

-diffusion of water across selectively permeable membrane

-water diffuses form a lower to a higher concentration

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Solvent

a substance capable of dissolving other substances

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Solute

a dissolved substance

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Osmosis Tonicity

ability go a solution to cause a cell to gain to lose water

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Isotonic solution

-concentration outside = concentration inside

-no net water movement

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Hypertonic solution

concentration outside cell is greater than the concentration inside the cell

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Hypotonic solution

concentration outside cell is less that the concentration inside the cell

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Facilitated diffusion

-facilitated = to make easier

-larger molecules can be transported

-transport using transport proteins

-channel proteins

-some carrier proteins

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Active Transport

-uses ATP

-moves against the gradient

-low concentration => high concentration

-not spontaneous

-not carrier mediated

-formation of vessicles

-exocytosis = "out"

-endocytosis = "in"

-phagocytosis = "eat"

-pinocytosis = "drink"

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Exocytosis

-waste, proteins, & secretory products

-vesicle fuses with plasma membrane

-releases contents from cell

-vesicle fuses with plasma membrane (PM) => primary mechanism for growing plasma membrane

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Endocytosis

-material taken into the cell by forming vesicles derived from the plasma membrane

-3 types: phagocytosis, pinocytosis, receptor mediated endocytosis

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Phagocytosis

-"cell eating"

-cell engulfed large particle

-non-specific

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Pinocytosis

-"cell drinking"

-ingestion of fluid & dissolved material

-non-specific

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Receptor-Mediated Endocytosis

-receptor proteins in plasma membrane bind specific macromolecules outside the cell

-form coated pits

-fold inward to form vesicles

-fold inward to form vesicles

-main mechanism for uptake of macromolecules

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Metabolism

-sum of all chemical reactions of an organism -> maintains homeostasis

-an emergent property of life

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Catabolic Pathway

-breaking down complex molecules into simpler ones

-releases energy => exergonic

-ex: cellular respiration, hydrolysis

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Anabolic Pathway

-build complex molecules from simpler ones

-uses energy => endergonic

-ex: synthesis of proteins from amino acids, dehydration synthesis

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Energy

capacity to cause change

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Potential Energy

stored energy that hasn't been used yet