Term
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Definition
| Polymers with molecular weights exceeding 1,000 grams per mole. |
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Term
| What are proteins formed from? |
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Definition
| Proteins are formed from different combinations of 20 different amino acids. |
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Term
| What are nucleic acids formed from? |
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Definition
| Nucleic acids are formed from four kinds of nucleotide monomers linked together in long chains. |
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Term
| How macromolecules function and interact with other molecules depends on the properties of certain chemical groups in their monomers called: |
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Definition
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Term
| An optical isomer occurs when: |
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Definition
| A carbon atom has four different atoms or groups attached to it. |
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Term
| The functions of macromolecules is directly related to: |
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Definition
| Their three-dimensional shapes and to the sequences and chemical properties of their monomers. |
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Term
| Polymers are constructed from monomers by a series of reactions called: |
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Definition
| Condensation reactions (dehydration reactions; both terms refer to the loss of water). |
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Term
| Condensation reactions result in what type of bond between monomers? |
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Definition
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Term
| When polymers are formed, what is released? |
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Definition
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Term
| The reverse of a condensation reaction is called a: |
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Definition
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Term
| Hydrolysis reactions result in: |
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Definition
| The breakdown of polymers into their component monomers. |
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Term
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Definition
| Catalytic proteins that speed up biochemical reactions. |
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Term
| What are defensive proteins? |
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Definition
| Recognize and respond to non-self substances that invade the organism from the environment. |
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Term
| What are hormonal and regulatory proteins? |
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Definition
| Proteins that control physiological processes. |
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Term
| What are receptor proteins? |
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Definition
| Proteins that receive and respond to molecular signals from inside and outside the organism. |
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Term
| What are storage proteins? |
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Definition
| Proteins that store chemical building blocks--amino acids--for later use. |
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Term
| What are structural proteins? |
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Definition
| Proteins such as collagen that provide physical stability and movement. |
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Term
| What are transport proteins? |
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Definition
| Proteins such as hemoglobin that carry substances within the organism. |
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Term
| What are genetic regulatory proteins? |
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Definition
| Proteins that regulate when, how, and to what extent a gene is expressed. |
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Term
| All proteins consist of one or more ____ chains. |
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Definition
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Term
| What is a polypeptide chain? |
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Definition
| An unbranched (linear) polymer of covalently linked amino acids. |
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Term
| The composition of a protein refers to: |
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Definition
| The relative amounts of the different amino acids present in its polypeptide chains. |
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Term
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Definition
| Right (dextro) amino acid. |
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Term
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Definition
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Term
| There are four levels of protein structure: |
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Definition
| Primary, secondary, tertiary, and quaternary. |
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Term
| The precise sequence of amino acids in a polypeptide chain held together by peptide linkages constitutes what? |
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Definition
| The primary structure of a protein. |
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Term
| The peptide backbone of the polypeptide chain consists of the repeating sequence: |
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Definition
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Term
| The carboxyl group in an amino acid carries what kind of charge? |
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Definition
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Term
| The amino group in an amino acid carries what kind of charge? |
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Definition
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Term
| The secondary, tertiary, and quaternary are derived from what? |
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Definition
| The proteins primary structure--that is, the precise location of specific amino acids in the polypeptide chain. |
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Term
| Primary structure is established by what kind of bonds? |
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Definition
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Term
| A protein's secondary structure consists of: |
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Definition
| Regular, repeated spatial patterns in different regions of a polypeptide chain. |
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Term
| What are the two basic types of secondary structure? |
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Definition
| The alpha helix and the beta pleated sheet. |
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Term
| The interactions between R groups determine what structure? |
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Definition
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Term
| Hydrogen bonding between the amino and carboxyl groups is responsible for what structure? |
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Definition
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Term
| Covalent disulfide bridges can form between what? |
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Definition
| Specific cysteine side chains, holding a folded polypeptide in place. |
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Term
| What type of bond between side chains help stabilize folds in proteins? |
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Definition
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Term
| Ionic bonds can form between positively and negatively charged side chains forming what between amino acids? |
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Definition
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Term
| If a protein is heated slowly, the heat energy will disrupt only the weak interactions, causing what? |
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Definition
| Secondary and tertiary structure to break down. This is known as denaturing. |
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Term
| All the information needed to specify the unique shape of a protein is contained in its what? |
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Definition
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Term
| Many functional proteins contain two or more polypeptide chains called what? |
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Definition
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Term
| A proteins quaternary structure results from what? |
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Definition
| The ways in which subunits bind together and interact. |
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Term
| What forces, interactions, and bonds help hold subunits together? |
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Definition
| Hydrophobic interactions, van der Waals forces, hydrogen bonds, and ionic bonds. |
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Term
| The weak nature of the bonds, interactions, and forces between subunits allow for what? |
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Definition
| Small changes in the quaternary structure to aid the protein's function. Example: Hemoglobin's ability to carry oxygen. |
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Term
| The specificity of protein binding depends on what two general properties? |
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Definition
| Its shape and the chemistry of its exposed surface groups. |
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Term
| What conditions can alter the weak, noncovalent interactions in a protein? |
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Definition
| Increases in temperature, alterations in pH, high concentrations of polar substances, and nonpolar substances. |
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Term
| Increases in temperature cause what in the structure of a protein? |
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Definition
| Increases in temperature cause more rapid molecular movements and thus can break hydrogen bonds and hydrophobic interactions, thus weakening a protein's structure. |
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Term
| Alterations in pH can affect a protein in what ways? |
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Definition
| Alterations in pH can change the pattern of ionization of exposed carboxyl and amino groups in the R groups of amino acids, this disrupting the pattern of ionic attractions and repulsions. |
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Term
| High concentrations of polar substances can do what to a protein's structure? |
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Definition
| High concentrations of polar substances can disrupt the hydrogen bonding that is crucial to protein structure. |
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Term
| How do nonpolar substances affect a protein's structure? |
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Definition
| Nonpolar substances may disrupt normal protein structure in cases where hydrophobic groups are essential to maintain the structure. |
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Term
| When does denaturation become irreversible? |
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Definition
| Denaturation becomes irreversible when amino acids that were buried in the interior of the protein become exposed at the surface, causing a new structure to form or different molecules to bind to the protein. Example: boiling an egg is irreversible . |
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Term
| When is a polypeptide in danger of binding to the wrong substance? |
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Definition
| Following denaturation, and after a protein is made. |
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Term
| Eukaryotic cells have special classes of proteins that act to counteract threats to three-dimensional structure called what? |
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Definition
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Term
| What to chaperone proteins do? |
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Definition
| Prevent inappropriate interactions and enhance the appropriate ones. |
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Term
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Definition
| Carbohydrates are a large group of molecules that all have a similar atomic composition but differ greatly in size, chemical properties, and biological functions. |
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Term
| What are the three major biochemical roles of carbohydrates? |
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Definition
| They are a source of stored energy that can be released in a form usable by organisms, they are used to transport stored energy within complex organisms, and they serve as carbon skeletons that can be rearranged to form new molecules. |
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Term
| What are the four categories of biologically important carbohydrates? |
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Definition
| Monosaccharides, disaccharides, oligosaccharides, and polysaccharides. |
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Term
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Definition
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Term
| Monosaccharides include what? |
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Definition
| Glucose, ribose, and fructose. |
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Term
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Definition
| Two monosaccharides linked together by covalent bonds. |
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Term
| What are oligosaccharides? |
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Definition
| Saccharides made up of several (3-20) monosaccharides. |
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Term
| What are polysaccharides? |
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Definition
| Polymers made up of hundreds or thousands of monosaccharides. |
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Term
| `All living cells contain what monosaccharide? |
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Definition
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Term
| What is glucose used for? |
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Definition
| Glucose is used to to transport energy in humans. |
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Term
| Polysaccharides are connected by what? |
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Definition
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