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Proteins, Lipids, Carbohydrates and Nuceic Acids. Can be up to 100,000 Daltons |
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A long molecule consisting of many similar or identical building blocks covalently bonded. Made up of monomers |
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The building blocks of polymers. The type depends on the kind of macromolecule |
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Two monomers are joined by this reaction during which a water molecule is lost. A Hydrogen is lost from one while an OH is lost from the other. |
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Another name for a condensation reaction when two monomers join to form a plolymer and lose a water molecule. |
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How a polymer is broken down into the monomers which built it. It requires water to break the bonds of the polymer. |
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Include sugars and polymers of sugars. |
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Sugars of the form CH2O, Glucose is the most common. Simple sugars of 3, 5 or 6 Carbons. Join to form di and polysaccharides. Usually Carbon rings |
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Made up of two monosaccharides joined by a covalent bond, dehydration reaction. Most common is sucrose or table sugar. |
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The dehaydration reaction which covalently bonds two monosaccharides into a disaccharide. |
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Macromolecules made up of 100's to 1000's of monosaccharides. Some function as energy storage. |
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A storage polysaccharide of plants made up of glucose monomers. Created by alpha linkages so they are digestable by hydrolysis enzymes. |
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Animals store energy in this form. It is an extensively branched polymer of glucose. Stored in the liver and muscle. |
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A strong, structural polysaccharide found in plant cell walls. A polymer of glucose. Created by beta linkages which animals cannot digest. |
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Can form rings in both an alpha and a beta form. This ability makes it useful in forming both starches and cellulose. |
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Another structural polysaccharide found in arthropods as their exoskeleton. |
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Not made up of monomers. They have little or no affinity for water due to their non-polar, hydrocarbon structure. Made up of fats, phopholipids and steroids. |
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Not polymers but large macromolecules assembled thru a dehydration reaction. Made from glycerol and fatty acids. |
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An alcohol with three carbons each with a hydroxyl group. Part of a fat. |
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A long Carbon skeleton, 16-18 C long. One end has a carboxyl group which gives it the name fatty acid. Attached to that carboxyl group is the chain of C-H bonds. |
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Three fatty acids linked to a glycerol, also called a triglyceride |
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A fatty acid with no double bonds, saturated with H atoms. |
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A fatty acid with one or more double bonds. Due to the double bonds, there are less H atoms than in a saturated fatty acid. |
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To store energy, like gasoline. Fats have more than 2X the energy of carbohydrates, 9cal/gram opposed to 4cal/gram. |
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Has two, rather than three, fatty acid chains atttached to a glycerol with the addition of a phosphate group with a negative charge. This creates a hydrophillic head with hydrophobic tails. Form the lipid bilayer in cells. |
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Lipids with a C skeleton consisting of four fused rings. They vary based on the functional groups. Ex: Cholesterol |
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A steroid component in animal cell membranes. Also, a precursor of other steroids like hormones which control physiological functions. |
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Polymers constructed from the 20 amino acids called polypeptides. The most complex of the macromolecules due to 4 levels of structure. |
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Polymers of the 20 amino acids. Form the tens of thousands of proteins in humans and other organisms. |
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Organic molecules with a carboxyl and an amino group. Each asymmetrical C has a hydrogen, a carboxyl, an amino and a unique, functional R group. |
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The dehydration reaction between the carboxyl group of one amino acid and the amino group on another. |
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Created by the peptide bonds between amino acids. One end is the free carboxyl group (c terminus) the other end has a free amino group (N terminus) |
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Primary structure of a protein |
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The unique amino acid sequence in a polypeptide chain. Determined by genetic information. |
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Secondary protein structure |
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The repeated coiling and folding of a polypeptide chain. The result of Hydrogen bonds. Can form an alpha helix or a beta folded sheet. |
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The folding caused by the R groups interacting. Some, which are hydrophobic, fold inward. The hydrophillic portions fold outwards. Further held together by disulfide bridges between the SH groups on Cysteine. |
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The folding caused by multiple polypeptide chains formin a single protein. Not in all proteins. |
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The covalent bond between the SH groups on two cysteine R groups as part of tertiary structure. |
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When a protein unfolds and loses its native form. Can be caused by changes in salt concentration, pH, temp or other environmental change. |
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Chaperone proteins which act to help other proteins fold correctly. Protect the protein from denaturization. |
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Used to determine a proteins three-dimensional structure. |
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Deoxyribonucleic Acid, found in cells. Carries hereditary information from one generation to the next. Made up of nucleic acid monomers. |
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Ribonucleic Acid, used in protein systhesis and is the genetic info in viruses and some bacteria. Made from nucleic acids. |
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Nucleic acid polymers. Made up of nucleotides |
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Has 3 parts: A nitrogenous base, a pentose (5 Carbon sugar) and a phosphate group. Pyrimadine or purine. |
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A nitrogenous base. A ring of C and N. Cytosine, Thymine and Uracil. |
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A nitrogenous base, larger than a pyrimadine. Contains a six membered ring fused to a 5 member ring. Adenine and guanine. |
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A 5 carbon sugar found in DNA and RNA, DNA has a version with 1 less oxygen on it |
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A phosphate group on the free end in the nucleotide polymer |
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Has a hydroxyl group on its free end in DNA |
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Two polynucleotides twisted together as in DNA |
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The two sugar-phospahte backbones run in opposite 5' => 3' direction |
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The bases in DNA are bonded in a certain way. Adenine bonds to Thymine or Uracil in RNA while Cytosine bonds to Guanine |
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