Biological catalyst

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macromolecule
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There are Four major types of biological macromolecules that make up the human body: nucleic acids (DNA & RNA), Carbohydrates, Proteins and Fats
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polymer
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a long molecule consisting of many similar or identical monomers linked together by covalent bonds
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monomer
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the subunit that serves as the building block of a polymer
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enzyme
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a macromolecule serving as a catalyst, a chemical agent that increases the rate of a reaction without being consumed by the reaction. Most are proteins.
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dehydration reaction
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a chemical reaction in which 2 molecules become covalently bonded to each other with the removal of a water molecule
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hydrolysis
hydrolysis
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a chemical reaction that breaks bonds between 2 molecules by the addition of water; functions in disassembly of polymers to monomers
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carbohydrates
carbohydrates
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a sugar (monosaccharide) or one of its dimers (disaccharide) or polymers (polysaccharide)
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monosaccharide
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the simplest carbohydrate, active alone or serving as a monomer for disaccharides and polysaccharides. Also known as simple sugars, that are generally some multiple of CH2O
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disaccharide
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a double sugar, consisting of two monosaccharides joined by a glycosidic linkage formed by a dehydration reaction
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glycosidic linkage
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a covalent bond formed between two monosaccharides by a dehydration reaction
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polysaccharide
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Polymers of simple sugars covalently linked by glycosidic bonds
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starch
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a storage polysaccharide in plants, consisting entirely of glucose monomers joined by alpha glycosidic linkages
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glycogen
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an extensively branched glucose storage polysaccharide found in the liver and muscle of animals; the animal equivalent of starch
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cellulose
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a structural polysaccharide of plant cell walls, consisting of glucose monomers joined by beta glycosidic linkages
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chitin
chitin
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a structural polysaccharide, consisting of amino sugar monomers, found in many fungal cell walls and in the exoskeletons of all arthopods
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lipid
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Hydrophobic. Considered monomers. Any of a group of large biological molecules, including fats, phospholipids, and steroids, that mix poorly, if at all, with water. Provide an efficient form of energy storage.
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fat
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a lipid consisting of 3 fatty acids linked to one glycerol molecule; also called a triacylglycerol or a triglyceride.
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fatty acid
fatty acid
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a carboxylic acid with a long carbon chain; vary in length and in the number and location of double bonds; 3 fatty acids linked to a glycerol molecule form a fat molecule, also known as a triacyglycerol or a triglyceride
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triacylglycerol
triacylglycerol
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a lipid consisting of 3 fatty acids linked to one glycerol molecule; also called a fat or triglyceride
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saturated fatty acid
saturated fatty acid
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a fatty acid in which all carbons in the hydrocarbon tail are connected by single bonds, thus maximizing the number of hydrogen atoms that are attached to the carbon skeleton
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unsaturated fatty acid
unsaturated fatty acid
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a fatty acid that has one or more double bonds between carbons in the hydrocarbon tail. Such bonding reduces the number of hydrogen atoms attached to the carbon skeleton
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trans fat
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an unsaturated fat, formed artificially during hydrogenation of oils, containing one or more trans double bonds
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phospholipid
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a lipid made up of glycerol joined to 2 fatty acids and a phosphate group. The hydrocarbon chains of the fatty acids act as nonpolar, hydrophobic tails, while the rest of the molecule acts as a polar, hydrophilic head.; form bilayers that function as biological membranes
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steroids
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a type of lipid characterized by a carbon skeleton consisting of 4 fused rings with various chemical groups attached
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cholesterol
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a steroid that forms an essential component of animal cell membranes and acts as a precursor molecule for the synthesis of other biologically important steroids, such as many hormones
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catalyst
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a chemical agent that selectively increases the rate of a reaction without being consumed by the reaction.
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Polypeptide
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A chain of amino acids linked together by peptide bonds or dehydration reactions
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protein
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a biologically functional molecule consisting of one or more polypeptides folded and coiled into a specific 3D structure
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amino acid
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An organic molecule possessing both a carboxyl and an amino group; serve as monomers of polypeptides
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peptide bond
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the covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by dehydration reaction
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primary structure
primary structure
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the level of protein structure referring to the specific linear sequence of amino acids
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secondary structure
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regions of repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bonding between constituents of the backbone (not the side chains).
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alpha helix
alpha helix
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a coiled region constituting one form of the secondary structure of proteins, arising from a specific pattern of hydrogen bonding between the atoms of the polypeptide backbone (not the side chains)
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beta pleated sheet
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one of the secondary structure of proteins in which the polypeptide chain fold back and forth. 2 regions of the chain lie parallel to each other and are held together by hydrogen bonds between atoms of the polypeptide backbone (not the side chains).
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tertiary structure
tertiary structure
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The overall shape of a protein molecule due to interactions of amino acid side chains, including hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges
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hydrophobic interaction
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a type of weak chemical interaction caused when molecules that do not mix with water coalesce to exclude water
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disulfide bridge
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a strong covalent bond formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer
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quaternary structure
quaternary structure
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the particular shape of a complex, aggregate protein, defined by the characteristic 3D arrangement of its constituent subunits, each a polypeptide
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sickle-cell disease
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a recessively inherited human blood disorder in which a single nucleotide change in the beta globin gene causes hemoglobin to aggregate, changing red blood cell shape and causing multiple symptoms in afflicted individuals
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denaturation
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in proteins, a process in which a protein loses its native shape due to the disruption of weak chemical bonds and interactions, thereby becoming Biologically inactive; in DNA, the separation of the two strands of the double helix. Occurs under extreme (noncellular) conditions of pH, salt concentration or temperature
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chaperonin
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a protein complex that assists in the proper folding of other proteins
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gene
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a discrete unit of hereditary information consisting of a specific nucleotide sequence in DNA (or RNA, in some viruses)
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nucleic acid
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a polymer (polynucleotide) consisting of many nucleotide monomers; serves as a blueprint for proteins and, through the actions of proteins, for all cellular activities. the 2 types of nucleic acid are DNA and RNA
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deoxyribonucleic acid (DNA)
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a double-stranded, helical nucleic acid molecule, consisting of nucleotide monomers with a deoxyribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G) and thymine (T); capable of being replicated and determining the inherited structure of a cell's proteins
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ribonucleic acid (RNA)
ribonucleic acid (RNA)
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a type of nucleic acid consisting of a polynucleotide made up of nucleotide monomers with a ribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G), and uracil (U); usually single-stranded; functions in protein synthesis, gene regulation, and as the genome of some viruses
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polynucelotide
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a polymer consisting of many nucleotide monomers in a chain. The nucelotides can be those of DNA or RNA.
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nucleotide
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the building block of a nucleic acid, consisting of a 5 carbon sugar covalently bonded to a nitrogenous base and one or more phosphate groups
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pyrimidine
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1 of 2 types of nitrogenous bases found in nucleotides, characterized by a 6-membered ring. Cytosine (C), thymine (T) and uracil (U) are examples of these.
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purines
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1 of 2 types of nitrogenous bases found in nucleotides, characterized by a 6-membered ring fused with a 5-membered ring. Adenine (A) and guanine (G) are examples of these.
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deoxyribose
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the sugar component of DNA nucleotides, having 1 of fewer hydroxyl group than ribose, the sugar component of the RNA nucleotide
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ribose
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the sugar component of RNA nucleotides
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double helix
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the form of native DNA, referring to its 2 adjacent antiparallel polynucleotide strands wound around an imaginary axis into a spiral shape
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antiparallel
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referring to the arrangement of the sugar-phophate backbones in a DNA double helix (they run in opposite 5' -> 3' directions)
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Saturated fat
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All carbons in the hydrocarbon tail are connected by single bonds
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Unsaturated fat
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A fatty acid that has one or more double bonds between carbons in the hydrocarbon tail.
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What are 6 functions of Proteins?
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Structural support Storage Transport Cellular Communications Movement Defense against substaces
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Primary Protein Structure
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Primary structure - the sequence of amino acids in a protein Primary structure is determined by inherited genetic information
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Ester bond
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Phosphodiester bond
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ATP
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(adenosine triphosphate) main energy source that cells use for most of their work
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nitrogenous base
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What are the three types of Polymers?
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C - P - N Carbohydrates Proteins Nucleic Acids
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In which two ways do we classify monosaccharides?
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The location of the carbonyl group The number of carbons in the carbon skeleton
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Give two examples of 3 Carbon Sugars
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Aldose and Ketose
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What is the simplest form of starch?
What is the simplest form of starch?
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Amylose
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What are the three main types of Lipids?
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Triglycerides Phospholipids Steroids
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Enzymes
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Proteins that act as a catalyst to speed up chemical reactions
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What are the Four Levels of Protein Structure?
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Primary Secondary Tertiary Quaternary
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What determines Tertiary Structure?
What determines Tertiary Structure?
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Interactions between R Groups rather than interactions between backbone constituents
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What are the R groups that determine Tertiary Structure?
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Hydrogen Bonds Ionic Bods Hydrophobic Interactions van der Waals interactions
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What is Collagen?
What is Collagen?
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A fibrous protein consisting of three polypeptide coiled like a rope
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What determines the quaternary structure of a protein?
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When two or more poplypeptide chains form one macromolecule
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How many essential amino acids are there and what are they used for?
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There are 20 essential amino acids used to form a protein.
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Sulfhydryl Group
Sulfhydryl Group
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Phosphate Group
Phosphate Group
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What area the FOUR categories of organic molecules that make up all living things
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Nucleic Acids (DNA ; RNA) Carbohydrates Lipids or Fats hyc Proteins
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Monosaccharide
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The simplest carbohydrate, active alone or serving as a monomer for disaccharides and polysaccharides. Also known as simple sugars, the molecular formulas of monosaccharides are generally some multiple of CH2O.
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dissaccharide
dissaccharide
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A double sugar, consisting of two monosaccharides joined by dehydration synthesis.
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polysaccharide (Cellulose)
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A structural polysaccharide of cell walls, consisting of glucose monomers joined by ?-1, 4-glycosidic linkages. A major component of pant cell walls
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polysaccharide (glycogen)
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An extensively branched glucose storage polysaccharide found in the liver and muscle of animals; the animal equivalent of starch.
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Which monosaccharide is the energy storing molecule produced by photosynthesis. Two of these molecules combine to make glucose
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Glyceraldehyde
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Which monosaccharide is a major nutrient, central to cellular metobolism. It is broken down for energy in the process of cellular respiration. The carbon skeleton of this sugar can also be used to build many other organic molecules, including amino acids and fatty acids.
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Glucose
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Which monosaccharide combines with glucose to form lactose, the disaccharide in milk
Which monosaccharide combines with glucose to form lactose, the disaccharide in milk
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Galactose
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Which monosaccharide is sometimes called fruit sugar-- the one that makes apples and berries sweet. This monosaccharide is also used to make the disaccharide sucrose, or table sugar.
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Fructose
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Which monosaccharide is an important component of RNA and ATP. A modified form is used in building DNA.
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Ribose
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List the 4 categories of organic macromolecules that make up all living things and the main functions of each
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Explain how organic macromolecules are polymers made up of monomer subunits.
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Describe the hydrolysis process of breaking down organic macromolecules to monomer subunits.
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Relating to carbohydrates, distinguish between and give examples of monosaccharides, disaccharides, and polysaccharides.
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Relating to carbohydrates, Know which types of organism make the following polysachharides as well as the function of each: Cellulose, glycogen, chitin, starch
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Relating to carbohydrates, state the monomer subunits that make up carbohydrates.
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Relating to carbohydrates, State the name given to the bond between monosaccharides.
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Relating to lipids, Describe a major difference between carbohydrates and lipids
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Relating to lipids, Give examples of lipids and the function of eachTriglycerides (fats/oils), phospholipids, steroids, waxes
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Relating to lipids, State the subunits that make up fats.
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Relating to lipids, Describe a triglyceride molecule and state the name given to the bond between glycerol and a fatty acid
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Relating to lipids, distinguish between the structure of saturated and unsaturated fatty acids, and between monounsaturated and polyunsaturated fatty acids.
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Relating to nucleic acids, state the 2 kinds of nucleic acids
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Relating to nucleic acids, state the monomer subunits that make up nucleic acids
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Relating to nucleic acids, describe the molecular structure of a nucleotide
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Relating to nucleic acids, state the name given to the bond between nucleotides
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Relating to nucleic acids, explain the function of DNA
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Relating to nucleic acids, explain the function of RNA
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Relating to proteins, give examples of protein functions
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Relating to proteins, state the monomer subunits that make up proteins
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Relating to proteins, show the structural formula of an amino acid, including the amino group, the carboxyl group, and the R group.
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Relating to proteins, describe the hydrophilic/hydrophobic nature of each of the following types of amino acids: nonpolar, polar, and electrically charged
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Relating to proteins, state the name given to the bond between amino acids
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Relating to proteins, distinguish between a polypeptide and a protein
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Relating to proteins, specifically describe the four levels of protein structure that give proteins their specific shape: primary, secondary, tertiary, and quaternary structure
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Relating to proteins, describe what is meant by denaturation and renaturation of a protein.
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Relating to proteins, explain why proteins function best under optimum pH and optimum temperature conditions.
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