Cell Biology 1st exam-def.

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lacythecoolest
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Cell Biology 1st exam-def.
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2014-02-17 19:37:26
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cell biology
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1st exam, definitions; buff state bio 214
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  1. Central Dogma Theory
    • Every cell in the body has the same DNA
    • Different cells express different subset
  2. What determines all rxns in the cell?
    Plasma Membrane
  3. Simplest eukaryote:
    yeast
  4. Rough ER differences from smooth
    • Ribosomes
    • protein synthesis
  5. Smooth ER differences from Rough
    • no ribosomes
    • lipid synthesis
    • Ca2+ storage
  6. Cytosol:
    Solutions with dissolved substances such as glucose, CO2, O2, ect.
  7. Cell fractionation:
    • takes cells apart and separates the major organelles from one another
    • -centrifuges and enables scientists to determine the functions of organelles
  8. Structure/Function Paradigm:
    the shape dictates the function
  9. Bioenergetics
    • Order and work requires energy
    • external energy must be converted into usable forms
  10. Central DOgma of Molecule Biology
    DNA->RNA->Proteins
  11. Plasma Membrane Comp and Func:
    • Phospholipid bilayer with embedded proteins
    • Selective passage of molecules into and out of cell
  12. Nucleus comp and func:
    • Nuclear envelope surrounding nucleoplasm, chromatin, and nucleolus
    • Storage of genetic information
  13. Nucleolus comp and func:
    • Located within nucleus
    • Concentrated area of chromatin, RNA, and proteins
    • Site for ribosome synthesis
  14. Ribosome comp and func:
    • Protein and RNA in two subunits
    • Protein synthesis
  15. Endoplasmic reticulum comp and func:
    • Membranous saccules and canals
    • Synthesis and/or modification of proteins and other substances, and transport by vesicle formation
  16. Smooth ER comp and func:
    • Having no ribosomes
    • Various; lipid synthesis in some cells
  17. Golgi apparatus comp and func:
    • Stack of membranous saccules
    • Processing, packaging, and distribution of molecules
  18. Vacuole and vesicle comp and func:
    • membranous sacs
    • Storage and transport of substances
  19. Lysosome comp and func:
    • Membranous vesicle containing digestive enzymes
    • Intracellular digestion
  20. Mitochondrion comp and func:
    • Inner membrane(with cristae) within outer membrane
    • Cellular respiration
  21. Cytoskeleton comp and func:
    • Microtubules, actin filaments, and intermediate filaments
    • Shape of cell and movement of its parts
  22. Cilia and flagella comp and func:
    • pattern of microtubules
    • Movement of cell
  23. Centriole comp and func:
    • pattern of microtubules
    • Formation of basal bodies
  24. Magnification
    the ratio of an object's image size to its real size
  25. Resolution
    The measure of the clarity of the image or the minimum distance of two distinguishable points
  26. Contrast
    Visible differences in parts of the sample
  27. Total surface area equation:
    (height x width) x sides x number of boxes
  28. Total volume equation:
    Height x width x length x number of boxes
  29. Surface to volume ratio equation
    surface area / volume
  30. Brightfield Stained
  31. Brightfield unstained
  32. Confocal
  33. Deconvolution
  34. Differential Interference Contrast
  35. Electron Microscopy
  36. Fluorescence
  37. Phase contrast
  38. Super-resolution
  39. Who came up with the term cells and when?
    Robert Hook 1665
  40. First person to see "animalcules" under the microscope and when?
    Van Leeuwennhoek, 1674
  41. Acid
    A molecule that releases a proton when dissolved in water; this dissociation generates hydronium(H30+) ions, thereby lowering the pH.
  42. Amino Acid
    • Functional group (-NH2)
    • Can accept a proton and carry a positive charge in aqueous solution.
  43. Atom
    The smallest particle of an element that still retains its distinctive chemical properties; consists of a positively charged nucleus surrounded by a cloud of negatively charged electrons
  44. Atomic Weight
  45. ATP
    • Adenosine 5-triphosphate
    • Molecule that serves as the principal carrier of energy in cells; this nucleoside triphosphate is composed of adenine, ribose, and three phosphate groups
  46. Avogadro's number
    The number of molecules in a mole, the quantity of a substance equal to its molecular weight in grams; approximately 6x10^23
  47. base
    Molecule that accepts a proton when dissolved in water; also used to refer to the nitrogen-containing purines or pyrimidine's in DNA and RNA
  48. buffer
    Mixture of weak acids and bases that maintains the pH of a solution by releasing and taking up protons
  49. chemical bond
    An exchange of electrons that holds two atoms together. Types found in living cells include ionic bonds, covalent bonds, and hydrogen bonds.
  50. Chemical group
    Combination of atoms, such as a hydroxyl group (-OH) or an amino group (-NH2), with distinct chemical and physical properties that influences the behavior of the molecule in which it resides
  51. Condensation reaction
    Chemical reaction in which a covalent bond is formed between two molecules as water is expelled; used to build polymers, such as proteins, polysaccharides, and nucleic acids.
  52. Conformation
    Precise, three-dimensional shape of a protein or other macromoluecule, based on the spatial location of its atoms in relation to one another
  53. Covalent bond
    Stable chemical link between two atoms produced by sharing one or more pairs of electrons
  54. DNA
    • Deoxyribonucleic Acid
    • Double-stranded polynucleotide formed from two separate chains of covalently linked deoxyribonucleotide units. It serves as the cell's store of genetic information that is transmitted from generation to generation.
  55. Electron
    Negatively charged subatomic particle that occupies space around an atomic nucleus
  56. Electrostatic attraction
    Force that draws together oppositely charged atoms. Examples include ionic bonds and the attractions between molecules containing polar covalent bonds
  57. fatty acid
    Molecule that consists of a carboxylic acid attached to a long hydrocarbon chain. Used as a major source of energy during metabolism and as a starting point for the synthesis of phospholipids.
  58. hydrogen bond
    A weak noncovalent interaction between a positively charged hydrogen atom in one molecule and a negatively charged atom, such as nitrogen or oxygen, in another; these interactions are key to the structure and properties of water
  59. hydrolysis
    Chemical rxn that involves cleavage of a covalent bond with the accompanying consumption of water
  60. Hydronium IOn
    The form taken by a proton (H+) in aqueous solution
  61. Hydrophilic
    Molecule or part of a molecule that readily forms hydrogen bonds with water, allowing it to dissolve; literally, "water loving"
  62. Hydrophobic
    Nonpolar, uncharged molecule or part of a molecule that forms few or no hydrogen bonds with water molecules and therefore does not dissolve; "water fearing"
  63. Hydrophobic interactions
    Type of noncovalent bond that forces together the hydrophobic portions of dissolved molecules to minimize their disruption of the hydrogen-bonded network of water; helps push together membrane phospholipids and fold proteins into a compact, globular shape
  64. Inorganic molecule
    Not composed of carbon and hydrogen
  65. Ion
    An atom carrying an electrical charge, either positive or negative
  66. Ionic bond
    Interaction formed when one atom donates electrons to another; this transfer of electrons causes both atoms to become electrically charged
  67. Lipid
    Organic molecule that is insoluble in water but dissolves readily in nonpolar organic solvents; typically contains long hydrocarbon chains or multiple rings.
  68. Lipid bilayer
    Thin pair of closely juxtaposed sheets, composed mainly of phospholipid molecules, that forms the structural basis for all cell membranes
  69. Macromolecule
    Polymer built from covalently linked subunits; includes proteins, nucleic acids, and polysaccharides with a molecular mass greater than a few thousand daltons
  70. Molecule
    Group of atoms joined together by covalent bonds
  71. Molecular weight
    Sum of the atomic weights of the atoms in a molecule; as a ratio of molecular masses, it is a number without units.
  72. Monomer
    Small molecule that can be linked to others of a similar type to form a larger molecule (polymer)
  73. Noncovalent bond
    Chemical association that does not involve th sharing of electrons; singly are relatively weak, but can sum together to produce strong, highly specific interactions between molecules. Examples are hydrogen bonds and van der Waals attractions
  74. Nucleotide
    Basic building block of the nucleic acids, DNA and RNA; includes a nucleoside with a series of one or more phosphate groups linked to its sugar
  75. Organic molecule
    Chemical compound that contains carbon and hydrogen
  76. pH scale
    Concentration of hydrogen ions in a solution, expressed as a logarithm. Thus, an acidic solution with pH3 will contain 10^-3 M hydrogen ions
  77. polar
    In chemistry, describes a molecule or bond in  which electrons are distributed unevenly
  78. Polymer
    Long molecule made by covalently linking multiple identical or similar subunits (monomers).
  79. Protein
    Polymer built from amino acids that provides cells with their shape and structure and performs most of their activities
  80. Proton
    Positively charged particle found in the nucleus of every atom; also, another name for a hydrogen ion (H+)
  81. RNA
    • Ribonucleic Acid
    • Molecule produced by the transcription of DNA
    • usually single-stranded, it is a poluculeotide composed of covalently linked ribonucleotide subunits.
  82. Sequence
    The linear order of monomers in a large molecule, for example amino acids in a protein or nucleotides in DNA; encodes info that specifies a macromolecules's precise biological func.
  83. Subunit
    A monomer that forms par of a larger molecule, such as an amino acid residue in a protein or a nucleotide residue in a nucleic acid.
  84. Sugar
    A substance made of carbon, hydrogen, and oxygen with a general formula(CH20)n.
  85. van der Waals attractions
    Weak noncovalent interaction, due to fluctuating electrical charges, that comes into play between two atoms within a short distance of each other
  86. Acetyl CoA
    Activated carrier that donates the carbon atoms in its readily transferable acetyl group to many metabolic rxns, including the citric acid cycle and fatty acid biosynthesis; the acetyl group is linked to coenzyme A by a thioester bond that releases a large amount of energy when hydrolyzed
  87. Activated carrier
    A small molecule that stores energy or chemical groups in a form that can be donated to many different metabolic rxns.
  88. Activation Energy
    The energy that must be acquired by a molecule to undergo a chemical rxn
  89. ADP, ATP
    • Adenosine diphosphate
    • Adenosine triphosphate
  90. anabolism
    Set of metabolic pathways by which large molecules are made from smaller ones
  91. Biosynthesis
    An enzyme-catalyzed process by which complex molecules are formed from simple substances by living cells; also called anabolism
  92. Catabolism
    Set of enzyme-catalyzed reactions by which complex molecules are degraded to simpler ones with release of energy.
  93. Catalysis
    Substance that accelerates a chemical rxn brought about by the action of a catalyst; virtually all rxns in a cell require such assistance to occur under conditions present in living organisms
  94. Catalyst
    Substance that accelerates a chemical rxn by lowering its activation energy; enzymes perform this role in cells
  95. Condensation Rxn
    Chemical reaction in which a covalent bond is formed between two molecules as water is expelled; used to build polymers, such as proteins, polysaccharides, and nucleic acids
  96. Coupled reaction
    Linked pair of chemical rxns in which free energy released by one rxn serves to drive the other rxn
  97. diffusion
    Process by which molecules and small particles move from one location to another by random, thermally driven motion
  98. Entropy
    • Thermodynamic quantity that measures the degree of disorder in a system
    • All transfers increase disorder to the universe
  99. Enzyme
    A protein that catalyzes a specific chemical rxn
  100. Equilibrium
    State in which the forward and reverse rates of a chemical rxn are equal so that no net chemical change occurs
  101. Equilibrium constant, K
    For a reversible chemical rxn, the ratio of substrate to product when the rates of the forward and reverse rxns are equal
  102. Free energy, G
    Energy that can be harnessed to do work, such as driving a chemical rxn
  103. free-energy change, changeG
    • in a chemical rxn, the difference in free energy between reactant and product molecules.
    • Large neg vaule of G = strong tendency to occur
    • Measurement of concentration, temperature and pressure
  104. Hydrolysis
    Chemical rxn that involves cleavage of a covalent bond with the accompanying consumption of water
  105. Metabolism
    The sum total of the chemical rxns that take place in the cells of a living organism
  106. Michaelis constant
    Concentration of substrate at which an enzyme works at half its maximum velocity; serves as a measure of how tightly the substrate is bound
  107. Oxidation
    Removal of electrons from an atom, as occurs during the addition of oxygen to a carbon atom or when a hydrogen is removed from a carbon atom
  108. Photosynthesis
    The process by which plants, algae, and some bacteria use the energy of sunlight to drive the synthesis of organic molecules from carbon dioxide and water
  109. Reduction
    Addition of electrons to an atom, as occurs during the addition of hydrogen to a carbon atom or the removal of oxygen from it
  110. Respiration
    General term for any process in a cell in which the uptake of molecular oxygen is coupled to the production of CO2
  111. Standard free-energy change
  112. substrate
    A molecule on which an enzyme acts
  113. turnover number
    The number of substrate molecules an enzyme can convert into product per second
  114. The process of making polymers
    polymerication
  115. what creates order to the universe?
    Thermal Dynamic
  116. What do you call a polysaccharide linkage?
    Glycosidic Linkage
  117. Amino Acids make?
    Proteins
  118. Nucleotides make?
    • Nucleic Acid
    • DNA
    • RNA
  119. Simple Sugars make:
    • Carbohydrates
    • saccharides
  120. Fatty acids make:
    • Lipids
    • glycerol
    • steroids
    • cholesterol
  121. What is a lipid linkage called?
    Ester Linkage
  122. What is the special bond in phospholipids?
    Phosphate bond
  123. What are the two ways a phospholipid form?
    • Micelle
    • Bilayer
  124. Name for when something is both hydrophobic and hydrophilic
    Ampaphatic
  125. What prevents our cells from freezing in the winter?
    • monosaturated fatty acid
    • Cholesterol signalers
  126. Special structure of steriods
    4 fused rings
  127. Nucleotide linkage:
    Phosphodiester Linkage
  128. Why is ATP such a great energy source?
    Because it has 3 negative energies, readily wants to repel them
  129. Adenine
  130. cytosine
  131. guanine
  132. thymine
  133. Pyrimidines
    • Thymine
    • Cytosine
  134. Purines:
    • Adenine
    • Guanine
  135. Nonpolar Amino acids
    • Alanine
    • Leucine
    • Isoleucine
    • Proline
    • Cysteine
    • Methionine
    • Phenylalanine
    • Tryptophan
    • Glycine
    • Valine
  136. Uncharged polar amino acids
    • Asparagine
    • Serine
    • Threonine
    • Tyrosine
    • Glutamine
  137. Positively charged amino acids
    • Histidine
    • Lysine
    • Arginine
  138. Negatively charged amino acids
    • Aspartic Acid
    • Glutamic Acid
  139. Amino acids form what type of bond?
    Peptide bond
  140. Amino acid functions
    • * proteins
    • * Peptide bonds
    • * Bacterial cell walls
    • * Antibiotics
    • * Signal molecule in brain
  141. Amino Acids Bond Types:
    • Peptide Bond
    • Polar Covalent
    • Condensation
  142. Amino Acid structure
    N-C-COOH
  143. Amino Acids Polymer
    Proteins
  144. Nucleotides Functions
    • DNA
    • RNA
    • ATP
  145. Nucleotides Bond Types
    • Phosphodiester Linkage
    • Covalent
    • Hydrogen bonding
  146. Nucleotides Polymers
    • Nucleic Acid
    • DNA
    • RNA
  147. Monosaccharides bonding type
    • Glycosidic Linkage
    • Covalent
    • Hydrogen Bonding
  148. Saccharides structure
    • (CH(2)O)n
    • N=3,4,5,6
    • Isomers
    • Ring formations
  149. Monosaccharides polymers
    • Carbohydrates
    • Disaccharides
    • Oligosaccharides
    • POlysaccharides
  150. Carbohydrates Functions
    • Production & storage of energy
    • Plant cell walls
    • insect exoskeletons
    • slime & mucus
    • Plasma Membrane
  151. Fatty Acids polymers, but not a polymer
    • Fats
    • membrane lipids
    • phospholipids
    • triacylglycerols
    • Steroids
    • Cholesterol
  152. Fatty Acids function
    • primary building block of all membranes
    • energy source
  153. Fatty acids bond type
    • Ester Linkage
    • Amphipathic
  154. Cell Wall
    Composed of Carbohydrates: cellulose or chitin
  155. Peroxisome
    Involved in hydrogen peroxide synthesis and degradation
  156. Chloroplast
    site of photosynthesis
  157. Schromoplast
    non-green pigments
  158. Leukoplast
    Stores starch
  159. Metabolism
    Series of chemical rxns involved in storing (anabolism) or releasing (catabolism) energy
  160. Glycolysis
    Anaerobic process in cytoplasm in which glucose, a 6 carbon compound, is oxidized to two pyruvates, which are both three carbon chains
  161. Krebs cycle
    Aerobic process that oxidizes pyruvates to CO2
  162. Gene functions
    • 1. to be preserved and transmitted
    • 2. to control various biological functions through the production of proteins and RNA
  163. Gene Structure
    • DNA
    • RNA
  164. Nucleotides
    • the components of nucleic acids, three subunits
    • 1. Sugar
    • 2. Phosphate
    • 3. Nitrogenous base
  165. How many different proteins are there?
    over 30,000
  166. Endogonic
    • Anabolic
    • creates order
    • requires energy
  167. Exergonic
    • Catabolic
    • breaks down,

    release energy
  168. dehydrogenase
    an enzyme that oxidizes a substrate by a reduction rxn that transfers one or more hydrides (H-) to an electron acceptor
  169. ATP
  170. Closed system
    a physical system which doesn't exchange any matter with its surroundings, and isn't subject to any force whose source is external to the system
  171. Open system
    a system which continuously interacts with its environment or surroundings
  172. Bioenergetics
    the study of how organisms manage their energy resources
  173. The Chemistry of Lie is organized into Metabolic Pathways
    Metabolism: totality of an organisms chem rxns

    Metabolic Pathway: begins w/a specific molecule and ends w/a product
  174. 3 kinds of kinetic energy
    • -movement
    • -thermal energy
    • -light energy
  175. Energy is:
    the capacity to cause change
  176. Potential energy is:
    energy that matter possesses because of its location or structure
  177. Types of potential energy:
    • -Chemical energy
    • -Positional energy
  178. The 5 Laws of Energy Transformation
    • 1. Thermodynamics
    • 2. Isolated system
    • 3. Open system 
    • 4. Organisms are open systems
    • 5. These laws apply to the universe as a whole
  179. 2 Laws of Thermodynamics
    1. Law of Conservation of Energy
  180. Law of Conservation of Energy
    • 1. The energy of the universe is constant
    • -energy can be transferred and transformed from one form to another, cannot be created or destroyed

    2. Implication-must account for source and fate of all energy in biological systems
  181. Law of Entropy
    • During every energy transfer or transformation, some energy becomes unusable, often lost as heat.
    • -Every transfer or transformation increases disorder(entropy)
    • -Entropy tends to increase in closed systems
    • -for a process to occur spontaneously, it must increase the entropy of the universe
  182. Energy flows into an ___________ in the form of _________ and exits in the form of _________
    • ecosystem
    • light
    • heat
  183. Cells create ordered __________ from less ordered ______
    • structures
    • materials
  184. Organisms replace ordered forms of ________ and _______ with less ordered forms
    • Matter
    • Energy
  185. The evolution of more complex organisms does not violate the ____ ___ __ ___________
    second law of thermodynamics
  186. Oxidation/Reduction Rxn Definition:
    The transfer of partial transfer of an electron from one atom to another
  187. Photosynthesis energy input and output
    • Sunlight->Heat
    • H20->O2
    • CO2->glucose
  188. Cellular Respirations energy inputs and outputs
    • Glucose->CO2 & heat
    • O2->H2O
    • ADP->ATP
  189. What does ATP do after created from cellular respiration?
    Cellular work and heat
  190. What products become oxidized and reduced  in this equation:

    CH4 + 2O2 = CO2 + energy + 2H2O
    • Oxidized: CH4 -> CO2
    • Reduced: 2O2 ->2 H2O
  191. 2 of the most stable molecules(as in oxidization/reduction)
    • CO2
    • H2O
  192. How does a exergonic rxn proceed?
    with a net release of free energy and is spontaneous
  193. How does an endergonic rxn proceed?
    absorbs free energy from its surroundings and is nonspontaneous
  194. Free energy chemical rxns proceed.....
    in direction that causes a loss in free energy which increases in net disorder
  195. Gibbs Free energy is
    a measure of a system's total energy available to do work, w/o reference to the surroundings
  196. Endergonic=positive G=is the rxn spontaneous or not
    no
  197. Exergonic=negative G=is the rxn spontaneous or not
    yes
  198. Coupled rxns
    When the net change of G is negative, the rxns are spontaneous
  199. In a Na Cl rxn what gets oxidized and what gets reduced. Also which is negative ion and which is the positive ion?
    • Na+ is the positive ion that gets oxidized
    • Cl- is the negative ion that gets reduced
  200. Rxns in a ______ system eventually reach _______ and then do _ _____
    • closed system
    • equilibrium
    • no work
  201. Cells are ___ in ________; they are ____ systems experiencing a constant flow of materials
    • not in equilibrium
    • open
  202. A defining feature of life is that ________ is never at __________
    • metabolism
    • equilibrium
  203. A ________ pathway in a cell releases ______ _______ in a series of rxns
    • catabolic
    • free energy
  204. ATP powers cellular work by coupling __________ rxns to __________ rxns
    • exergonic
    • endergonic
  205. 3 main kinds of work a cell does
    • -chemical
    • -transport
    • -mechanical
  206. To do work, cells manage energy resources by ________ _________
    energy coupling
  207. Most energy coupling in cells is mediated by ___
    ATP
  208. Why is there so much energy in ATP?
    the negative charges don't like being so close
  209. What can break the phosphate bonds in ATP?
    Hydrolysis
  210. WHen is energy released from ATP?
    when the terminal phosphate bond is broken
  211. Where does the energy come from when the phosphate bond in ATP is broken?
    chemical change to a state of lower free energy
  212. What happens when change in G=0?
    no energy
  213. 3 high energy electron carriers:
    • 1. NAD+ -> NADH
    • 2. NADP+ -> NADPH
    • 3. FAD -> FADH2
  214. ________ speed up metabolic rxns by __________ energy barriers
    • Enzymes
    • Lowering
  215. A chemical agent that speeds up a reaction without being consumed by the reaction
    Catalyst
  216. A catalytic protein
    Enzyme
  217. The initial energy needed to start a chemical rxn is called:
    activation energy
  218. __________ ___________ is often supplied in the form of thermal energy that the reactant molecules absorb from their surroundings
    Activation Energy
  219. Nonprotein enzyme helpers
    cofactors
  220. An organic cofactor is called a:
    coenzyme
  221. What randomness does coenzymes include?
    vitamins
  222. What binds to the active site of an enzyme, competing with the substrate?
    Competitive inhibitors
  223. What binds to ANOTHER part  of an enzyme to change shape and make the active site less effective?
    Noncompetitive inhibitors
  224. What are some examples of inhibitors?
    toxin, poisons, pesticides and antibiotics
  225. ________ _____ store, transmit, and help express hereditary information
    Nucleic acids
  226. The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a:
    gene
  227. ______ are made of DNA
    Genes
  228. Nucleic acid made of monomers called:
    nucleotides
  229. _____ provides directions for its own replication
    DNA
  230. DNA directs synthesis of ______ and through _____ controls protein synthesis
    mRNA
  231. What do nucleic acids do?
    • store & transmit hereditary information
    • regulate gene expression
  232. What are the two super charged molecules in DNA & RNA that repel each other?
    Phosphate group & Nitrogenous base
  233. Enzymatic Protein func and ex
    • Selective acceleration of chem rxns
    • EX: digestive enzymes catalyze the hydrolysis of bonds in food molecules
  234. Defensive proteins func & ex
    • Protection against disease
    • ex: antibodies inactivate and help destroy viruses and bacteria
  235. Storage proteins func & ex
    • Storage of amino acids
    • ex: Plants of storage proteins in their seeds
  236. Transport proteins func & ex:
    • Transport of substances
    • ex: hemoglobin, iron protein->oxygen from lungs to body
  237. Hormonal Protein func & ex
    • Coordination of an organism's activities
    • ex: insulin, causes other tissues to up take glucose which regulates blood sugar concentration
  238. Receptor Proteins func & ex
    • Response of cell to chemical stimuli
    • Ex: built into membrane of nerve cell detect signaling molecules released by other nerve cells
  239. Contractile and motor proteins func & ex
    • Movement
    • ex: actin and myosin proteins are responsible for the contraction of muscles
  240. Structural proteins func & ex:
    • Support
    • Keratin, collagen, elastin and silk fibers
  241. What do you call a polysaccharide(carbohydrates) linkage?
    Glycosidic LInkage
  242. What do you call a lipid linkage?
    Ester LInkage
  243. What do call a nucleic acid linkage?
    phosphodiester
  244. What do you call a amino acid linkage?
    Peptide Linkage
  245. 4 basic monomers
    • amino acid
    • fatty acid
    • nucleic acid
    • monosaccharides
  246. How do you form a peptide bond?
    OH and H of two amino acids and connect the C and N together
  247. The four bonds involved in the folding and maintence of proteins:
    • Hydrogen bonds
    • Electrostatic attractions
    • Van der Waals
    • Hydrophobic interaction
  248. The final folded structure of a protein is called:
    conformation
  249. When a protein refolds spontaneously to its original conformation after its been denatured
    renaturation
  250. Molecule that steers proteins along productive folding pathways, helping them to fold correctly and preventing them from forming aggregates inside the cell
    chaperone protein
  251. The primary structure of a protein:
    Amino acid sequence
  252. Secondary Structure of a protein:
    Folds that form in certain segments of the polypeptide chain
  253. Tertiary Structure of the protein:
    full, three-dimensional conformation of the entire polypeptide chain
  254. Quarternary Structure of a protein:
    More than one polypeptide chain
  255. regions of polypeptide chain lacking any definite structure
    intrinsically disordered sequences
  256. Shape name in which the polypeptide chain folds up into a compact shape like a ball with an irregular surface
    Globular Proteins
  257. Shape name for protein that have a relatively simple, elongated three-dimensional structure
    fibrous proteins
  258. Most abundant fibrous protein
    collagen
  259. A substance that is bound by a protein
    ligand
  260. Region of a protein that associates with a ligand
    binding site
  261. Enzymes that catalyze a hydrolytic cleavage rxn
    hydrolase
  262. Enzyme class that breaks down nucleic acids by hydrolyzing bonds btwn nucleotides
    nuclease
  263. Enzyme class that breaks down proteins by hydrolyzing peptide bonds btwn amino acids
    protease
  264. Enzyme class that joins two molecules together
    Ligase
  265. Enzyme class that catalyzes the rearrangement of bonds within a single molecule
    Isomerase
  266. Enzyme class that catalyzes polymerization reactions such as the synthesis of DNA and RNA
    Polymerase
  267. Enzyme class that catalyzes the addition of phosphate groups to molecules
    Kinase
  268. Enzyme class that catalyzes the hydrolytic removal of a phosphate group from a molecule
    Phosphatase
  269. Enzyme class tha catalyze rxns in which one molecule is oxidized white the other is reduced
    oxido-reductase
  270. Enzyme class that hydrolyzes ATP
    ATPase

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