Molecular and Cellular Biology Exam 1

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144 Terms

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bright field microscope

requires staining to improve contrast

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phase contrast microscope

enhances contrast of transparent specimens without staining

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DIC microscope

produces 3D like images of unstained live specimens

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fluorescence microscope

utilizes fluorescent dyes or proteins for visualization of specific molecules or structures in cells

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confocal microscope

uses lasers and small apertures to eliminate out of focus light for sharper 3D reconstructions, higher resolution

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electron miscroscope

uses electron beams

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transmission electron microscope

electrons pass through ultrathin sections of specimen, reveals fine internal structures

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scanning electron microscope

electrons scan specimen surface, produces detailed 3D images of surfaces

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cryogenic sample electron microscopy

freeze biological samples rapidly in a layer of vitreous ice, electrons hit biological samples frozen in a layer of vitreous ice, produces 3D structures of molecules such as proteins and nucleic acids

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atomic force microscopy

scans specimen surface with a physical probe, provides nanometer scale topographic maps

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super-resolution microscopy

overcomes the diffraction limit of light, visualization of structures at high resolution

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what is composed of 30% chemicals and 70% water?

bacterial cells

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carbohydrate

biological macromolecule in which the ratio of carbon to hydrogen and to oxygen is 1:2:1

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monosaccharide (carbohydrate)

simple sugar

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disaccharide (carboyhydrate)

two monosaccharides that are covalently bonded

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polysaccharide (carbohydrate)

complex sugar or starch, large molecule composed of monosaccharides that are covalently bonded

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monosaccharide properties

usually 3-7 carbon atoms

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aldose

has aldehyde functional group, R-CHO

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ketose

has ketone functional group RC(=O)R’)

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triose

3 carbons

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pentose

5 carbons

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hexose

6 carbons

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structural isomers

same chemical formula, different arrangement of atoms

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disaccharides form when:

two monosaccharides undergo a dehydration reaction

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glycosidic bond

covalent bond between two monosaccharides

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sucrose

glucose + fructose

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lactose

glucose + galactose

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maltose

glucose + glucose

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polysaccharides in bacteria

cellulose

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polysaccharides in plants

starch and cellulose

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polysaccharides in fungi

chitin

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polysaccharides in animals

glycogen and chitin

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polysaccharides consist of:

a long chain of monosaccharides linked by glycosidic bonds, can be soluble or insoluble in water

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amylose

linear chain that is insoluble

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amylopectin

branched chain that is insoluble

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cellulose

structural component of a plant’s cell wall, a linear polysaccharide composed of glucose units linked by beta 1-4 glycosidic bonds

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glycogen

the stored form of glucose in humans and other vertebrates, highly branched, stored in liver and muscle cells, broken down into glucose when blood glucose decreases by a process called glycogenolysis

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lipids

a diverse group of compounds that are mostly nonpolar, are hydrophobic/insoluble

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lipids are composed of:

hydrocarbons with mostly nonpolar C-C or C-H bonds

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why are lipids important for life?

they store energy for long term use, provide insulation from the environment, are the building blocks of many hormones, and are components of cell membranes

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lipids produced by cells

fats and oils, waxes, phospholipids, and steroids

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fats (triglycerides)

composed of glycerol and three fatty acid chains

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saturated fats

no available position for hydrogen to bind, usually solid at RT

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unsaturated fats

double bonds allow for hydrogen to bind, usually liquid at RT (oils)

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unsaturated

has double bond, can be cis or trans

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ester bond formation

releases 3H2O

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saturated

all single bonds

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waxes

serve as water proofing for organisms, formed from fatty acid chains and long chain alcohols via esterification

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esterification

formation of ester bonds

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amphipathic molecules

are phospholipids, has hydrophobic and hydrophilic regions (polar phosphate head - hydrophilic) + (non-polar fatty acid tails - hydrophobic)

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steroids

organic molecule with 4 fused hydrocarbon ring structures (3 six-ring and one 5-ring), some with hydroxyl group, hydrophobic

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functions of steroids

hormones (testosterone and estrogen), stress response (cortisol), and structure, signaling and disease (cholesterol)

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5’ terminal

phosphate group at end

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3’ terminal

hydroxyl group at end

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nucleic acid

chains of nucleotides, building blocks of genetic information

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pyrimidines

one carbon-nitrogen ring

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purines

two carbon-nitrogen rings

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what is the most common form of DNA in cells?

B form

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proteins

macromolecules composed of one or more peptides (composed of amino acid subunits)

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parts of an amino acid:

animo group, carboxyl group, central carbon bonded to H atom, R group

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peptide bond

a type of covalent bond that links two amino acids

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primary protein structure

sequence of a chain of amino acids

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secondary protein structure

local folding of the polypeptide chain in helices or sheets

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tertiary protein structure

three-dimensional folding pattern of protein due to side chain interactions

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quarternary protein structure

protein consisting of more than one amino acid chain

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polypeptide secondary structure

folding of regions into specific structural patterns within a polypeptide chain

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polypeptide tertiary structure

three-dimensional arrangement of the entire polypeptide chain of a protein, including all its secondary structures in 3D space

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polypeptide backbone model

simple way to depict protein structure

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ribbon model

easier to identify secondary structures (alpha helices, beta sheets)

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wire model

shows amino acid side chains

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space filling model

easier to assess the size, shape of protein, and steric effects

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steric effects

non-bonding interactions that influence the shape of a molecule

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denaturation

process where a protein loses its quaternary, tertiary, and secondary structure without losing its primary sequence, can be reversible or irreversible

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causes of denaturation

external stress, exposure to certain compounds, heat, cell death

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similarities between prokaryotes and eukaryotes

cell membrane (plasma membrane), cytoplasm, ribosomes, DNA

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cytoplasm

cytosol + any other components except the DNA, contains ions and other macromolecules

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cytosol

liquid component of a cell

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cell wall (prokaryotes)

found in most prokaryotes, composed of peptidoglycan, wraps around the cell membrane, extra layer of protection, helps maintain cell shape and prevents dehydration

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capsule (prokaryotes)

composed of polysaccharides, enables cell to attach to surfaces

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flagella (prokaryotes)

whiplike structure, used for locomotion (can also be found in eukaryotic cells)

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pili (prokaryotes)

tube like structures, for exchanging genetic material during conjugation

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fimbriae (prokaryotes)

thread-like structures used to attach to a host or a surface

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mitochondria

site of Krebs cycle and electron transport chain

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rough endoplasmic reticulum

site of protein synthesis, modification, folding, and sorting proteins

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smooth endoplasmic reticulum

site of lipid synthesis

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golgi apparatus

sorts, tags, packages and distributes proteins and lipids

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vesicle

a structure within or outside a cell, consisting of liquid or cytoplasm enclosed by a lipid bilayer - may contain proteins, lipids, ions, and other organic molecules

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cell theory

cells arise from preexisting cells

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endosymbiotic theory

mitochondria and chloroplasts arose as a result of prokaryotic cells establishing a symbiotic relationship within a eukaryotic host

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catalyst

a substance that increases the rate of a reaction without being consumed

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enzyme

a catalyst that speeds up the rate of a biochemical reaction - most are proteins

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activation energy

minimum amount of energy that must be provided for compounds to result in a chemical reaction

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Gibbs free energy

energy available to do useful work in a system at constant temperature and pressure

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induced fit model

model that describes how enzymes function - when a substrate binds to the active site of an enzyme, the enzyme slightly changes its shape to better accommodate the substrate - creates a more precise fit - facilitates the chemical reaction

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conformational change

a change in the shape of a molecule such as a protein

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mechanisms for enzyme regulation

molecular regulation (inhibitors, activators, coenzymes and cofactors), compartmentalization, feedback inhibition

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enzyme inhibitors

molecules or substances that reduce the activity of an enzyme - leads to reduction in amount of products - substrates may accumulate

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competitive inhibition

a molecule or substance competes with the substrate for binding to an active site —> decreased enzyme activity - usually resembles the structure or shape of a substrate

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non-competitive inhibition

an inhibitor binds to the enzyme in a location other than the active site (allosteric site) —> decreased enzyme activity

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allosteric site

a location in an enzyme other than the active site that allows for regulation of enzyme activity