Cell and Molecular Biology Exam 1

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332 Terms

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7 Most Important Functional Groups for Life
hydroxyl, carbonyl, carboxyl, sulfhydryl, amino, phosphate, and methy, can replace hydrogen atoms attached to skeletons of organic molecules
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Acetyl CoA
activated carrier that donates the carbon atoms in its readily transferable acetyl group to many metabolic reactions, including the citric acid cycle and fatty acid biosynthesis; the acetyl group is linked to the coenzyme A (CoA) by a thioester bond that releases a large amount of energy when hydrolyzed
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Acid
A molecule that releases a proton when dissolved in water; this dissociation generates hydronium ions, thereby lowering the pH
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Acidic Side Chains
Aspartic Acid and Glutamic Acid, within cells, side chains will have negative charges and be able to form ionic bonds with basic amino acid residues and other ionized molecules. They enhance the water solubility of the polypeptide as they are able to interact with the positive dipoles of water and other molecules, can be phosphorylated
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Activated Carrier
a small molecule that stores energy or chemical groups in a form that can be donated to many different metabolic reactions, such as ATP, acetyl CoA, and NADH
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Activation Energy
the energy that must be acquired by a molecule to undergo a chemical reaction
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Active Site
region on the surface of an enzyme that binds to a substrate molecule and catalyzes its chemical transformation
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Active Site
the region on the enzyme where the substrate binds
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Adipose cells and tissue
humans and other mammals store their fat in adipose cells, adipose tissue also cushions vital organs and insulates the body
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ADP
nucleoside diphosphate produced by hydrolysis of the terminal phosphate of ATP
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Allosteric Inhibitors
bind to a region other than the active site (an allosteric site), they do not block the association of substrate with the active site, and they cause the enzyme to change shape to a less than optimal conformation
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Allosteric
describes a protein that can exist in multiple conformations depending on the binding of a molecule (ligand) at a site other than the catalytic site, such changes from one conformation to another often alter the protein's activity or ligand affinity
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Alpha glucose
polymers are helical
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Alpha Helices
Many membrane-bound proteins cross the lipid bilayer as an alpha helix, which is the dominant pattern for membrane-bound enzymes and receptor proteins, in which a single polypeptide chain twists around itself to form a rigid cylinder stabilized by hydrogen bonds between every fourth amino acid, intertwined alpha helixes can form a stiff coiled-coil
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Amino acid naming in a polypeptide chain
amino acid residues
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Amino Acid Sequence
the order of the amino acid subunits in a protein chain, sometimes called the primary structure of a protein
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Amino Acid
small organic molecule containing both an amino group and a carboxyl group; it serves as the building block of proteins
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Amino
(-NH2, -NH3+)
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Amphiphilic
possessing both hydrophilic and hydrophobic properties or sides
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Amylase
enzyme that digests starch by hydrolyzing alpha linkages, cannot hydrolyze beta linkages in cellulose. To break b linkages, an organism would need to express a cellulase like cellobiase (animals do not express cellulases)
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Amylopectin
a branched form of plant starch
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Amylose
simplest form of starch
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Anabolic Pathways
those that consume energy to build smaller molecules into larger ones and establish order (decrease entropy) within the living organism
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Anabolism
set of metabolic pathways by which large molecules are made from smaller ones
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Animal relationship with microbes that aid in cellulose digestion
symbiotic
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Anion
a negatively charged ion
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Antibody
protein produced by B lymphocytes in response to a foreign molecule or invading organism, binds to the foreign molecule or cell extremely tightly, thereby inactivating it or marking it for destruction
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Antigen
molecule or fragment of a molecule that is recognized by an antibody
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Apoenzyme
an enzyme on its own, without cofactors present, and inactive
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Aqueous Solution
one in which water is the solvent, concentration of solutes is critical for chemical reactions because higher concentration means more collisions
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Archaeon
Microscopic organism that is a member of one of the two divisions of prokaryotes; often found in hostile environments such as hot springs or brine
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Artificial Intelligence
has become a major force in the world of bioinformatics, reducing compute times by several orders of magnitude in many cases
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Asparagine and Glutamine
Polar side chains, similar to aspartate and glutamate (missing the -OH groups)
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Atom
the smallest particle of an element that still retains its distinctive chemical properties
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Atomic Force Microscope
drags a nano-scale probe across the surface of a specimen, detects bumps, valleys
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ATP Composition
composed ribose (sugar), adenine (a nitrogenous base), and three phosphate groups
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ATP
activated carrier that serves as the principal carrier of energy in cells; a nucleoside triphosphate composed of adenine, ribose, and 3 phosphate groups
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Avogadro's Number
the number of molecules in a mole, the quantity of a substance equal to its molecular weight in grams
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Bacillus
type of shape bacteria and archaea can adapt
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Bacterium
Microscopic organism that is a member of one of the two divisions of prokaryotes; some species cause disease
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Base
any substance that reduces the H+ concentration of a solution, molecule that accepts a proton when dissolved in water
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Basic Side Chains
Lysine, Arginine, and Histidine, can form ionic bonds and dipole interactions, enhance water solubility, can be phosphorylated, positive charges
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Beta glucose
polymers are straight
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Beta Sheet
folding pattern found in many proteins in which neighboring regions of the polypeptide chain associate side-by-side with each other through hydrogen bonds to give a rigid, flattened structure, form rigid structures at the core of many proteins, antiparallel Beta sheets are most common, but parallel beta sheets are also present, and can stack to form an amyloid structure that resembles the type of insoluble aggregates observed in the neurons of individuals with different neurodegenerative diseases
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Bilayer
the assembly that phospholipids take on when they are added to water with the hydrophobic tails pointing toward the interior, phospholipid bilayers are found in cell membranes
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Binding Site
region on the surface of a protein, typically a cavity or groove, that interacts with another molecule(a ligand) through the formation of multiple noncovalent bonds
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Bioinformatics
uses a computational approach to predict protein structure from amino acid sequences; this process is complex and requires significant computing power
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Biomolecular Condensate
A large aggregate of phase-separated macromolecules that creates a region with a special biochemistry without the use of an encapsulating membrane
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Biosynthesis
an enzyme-catalyzed process by which complex molecules are formed from simpler substances by living cells
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Bright-Field Microscopes
series of lenses for magnification, light passes through the specimen into the objective lens
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Buffer
mixture of weak acids and bases that maintains the pH of a solution by releasing and taking up protons
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C-Terminus
the end of a polypeptide chain that carries a free carboxyl group
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Capsule/ Slime Layer
adds protection, adhesion
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Carbohydrate
simple sugars and polymers of sugars, serve mainly as fuel and building material
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Carbonyl
(-COH, -CO-)
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Carboxyl
(-COOH, --COO)
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Catabolic Pathways
those that break down molecules to release energy and produce intermediate metabolites (smaller molecules that can be used to build up larger ones), release energy in a series of reactions, one reaction driving the next reaction
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Catabolism
set of enzyme-catalyzed reactions by which complex molecules degraded to simpler ones with release of energy; intermediates in these reactions are sometimes called catabolites
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Catalyst
substance that accelerates a chemical reaction by lowering the activation energy, enzymes perform this role in cells
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Cation
a positively charged ion
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Cell Respiration
process by which cells harvest the energy stored in food molecules; usually accompanied by the uptake of O2 and the release of CO2
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Cell Theory
At a minimum, cells consist of a membrane and the contents therein, all organisms are composed of 1 or more cells, cells are the basic living units of function and organization, and all cells come from other cells
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Cell Wall
tough structural reinforcement
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Cell
The basic unit from which a living organism is made; an aqueous solution of chemicals enclosed by a membrane; has an ability to self-replicate
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Cellular PrP
the healthy conformation; its functional domain is composed of alpha helices
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Cellulose
A structural polysaccharide, major component of the cell walls of plant, differs from starch by the glycosidic linkages
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Centrosomes
are the organizing centers of microtubules, important for mitosis
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Change in Free Energy During a Process Related to Enthalpy and Entropy
Delta G = DeltaH - TDeltaS
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Chaperones
helper proteins which are often needed to aid in proper folding of a polypeptides it's extruded from a ribosome; will prevent misfolding and ferry the polypeptide to the chaperonin
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Chaperonin
a complex structure that will accept a newly synthesized polypeptide into an inner chamber; will change shape, contorting the polypeptide within, giving it a new stable conformation
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Chemical Bond
an attraction that holds two atoms together
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Chemical Group
a combination of atoms with distinct chemical and physical properties that influence the behavior of the molecule in which it resides
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Chitin
another structural polysaccharide, is found in the exoskeleton of arthropods, also provides structural support for the cell walls of many fungi, unlike cellulose, animals can digest it, though very slowly
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Chloroplast
Specialized organelle in algae and plants that contains chlorophyll and serves as the site for photosynthesis
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Cholesterol
an important steroid, is a component in animal cell membranes, increases fluidity in cold environments and increases viscosity in hot environments, although essential to animals, high levels in the blood may contribute to cardiovascular disease
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Chromatography
technique used to separate the individual molecules in a complex mixture on the basis of their size, charge, or their ability to bind to a particular chemical group. In a common form of the technique, the mixture is run through a column filled with a material that binds the desired molecule, and it is the eluted from the column with a solvent gradient
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Chromosome
Long, threadlike structure composed of DNA and proteins that carries the genetic information of an organism; becomes visible as distinct entity when a plant or animal cell prepares to divide
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Cilia
are found on many cell types, used to move mucus/secretions normally
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Cis-Trans Isomers
have the same covalent bonds but differ in spatial arrangments
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Coenzyme
Organic cofactors, small molecule that binds tightly to an enzyme and helps it to catalyze a reaction
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Cofactors
like ions and other organic compounds (coenzymes) that most enzymes require to function, non-protein enzyme helpers
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Coiled-Coil
stable, rodlike protein structure formed when two or more alpha helices twist repeatedly around each other
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Colloid
a stable suspension of fine particles in a liquid
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Common Traits in Eukaryotes
one nucleus, complex cytoskeleton, mitochondria, plastids in photosynthesizers (chloroplasts)
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Competitive Inhibitors
molecules that bind to the active site of an enzyme, competing with the substrate, but if substrate concentration increases, it can outcompete the inhibitor, and the enzyme's maximal function will be restored
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Complementary Base Pairs
A pairs with T using 2 hydrogen bonds, G pairs with C using 3 hydrogen bonds, or A pairs with U using 2 hydrogen bonds
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Condensation Reaction
chemical reaction in which a covalent bond is formed between two molecules as water is expelled; used to bind polymers, such as proteins, polyssacharides, and nucleic acids
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Confocal Fluorescence Microscopes
use fluorescent dyes and lasers to image a single plane, emitted light passes through a pinhole aperture, increasing resolution, computer constructs a 3-D image from multiple images capturing different planes of the specimen (z-stack)
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Conformation
precise, three-dimensional shape of a protein or other macromolecule, based on the spatial location of its atoms in relation to one another
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Contractile/Motor Proteins
movement, i.e. motor proteins are responsible for the undulations of cilia and flagella, actin and myosin proteins are responsible for the contraction of muscles, protein such as myosin or kinesin that uses energy derived from the hydrolysis of a tightly bound ATP molecule to propel itself along a protein filament or other polymeric molecule
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Cooperativity
can amplify enzyme activity- once a substrate binds to one subunit, the other subunits can bind substrate more readily
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Coupled Reaction
linked pair of chemical reactions in which free energy released by one reaction serves to drive the other reaction
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Covalent Bonds
sharing of a pair of valence electrons by two atoms, atoms must remain close together in order for their valence shells to remain complete, strong and unaffected by the presence of water
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Cryo-Electron Microscopy (cryoEM)
technique for observing the detailed structure of a macromolecule at very low temperatures after freezing native biological structures in ice
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Cysteine
Polar side chains, contains a thiol group (-SH) and can form disulfide bridges (covalent bonds) with the thiol groups of other cysteine residues
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Cytoplasm
Contents of a cell that are contained within its plasma membrane but, in the case of eukaryotic cells, outside the nucleus
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Cytoskeleton
System of protein filaments in the cytoplasm eukaryotic cell that gives the cell shape and the capacity for directed movement; its most abundant components are actin filaments, microtubules, and intermediate filaments, anchors organelles, maintains cell structure, dynamically changes the shape of the cell, acts as transport lines for vesicles
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Cytosol
Contents of the main compartment of the cytoplasm, excluding membrane-enclosed organelles such as the endoplasmic reticulum and mitochondria
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Daltons
6.02 x 10^23 Da = 1 g, 1 Da is the mass of a proton or neutron
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Dangers of Enantiomers
important for drug development, Differing effects of enantiomers demonstrate that organisms are sensitive to even subtle variations in molecules, Usually only one drug enantiomer is considered so-called "biologically active" (meaning that this isomer was designed to have a desired effect on an organism), but both enantiomers will affect an organism in some manner, for example thalidomide