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Composed of a single element. |
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Composed of two or more elements in a fixed ratio. |
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Different number of neutrons. |
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Decay of an isotope by the splitting of a neutron into a proton and an electron. |
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Incomplete outer electron shell. |
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The number of electrons in the valence shell. |
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The sharing of electrons. |
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The loss or gain of electrons. |
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Ability of an atom to attract electrons. |
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Atoms have equal electronegativity. |
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Atoms have unequal electronegativity. The atom with the greater electronegativity gains a partial negative charge and the atom with the lesser electronegativity gains a partial positive charge. |
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Atoms with very high electronegativity "steal" electrons from atoms with much lower electronegativity. |
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Dipole-dipole interactions between hydrogen and small highly electronegative atoms. |
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Van der Waal Interactions |
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Electrons in two atoms influence each other to create a temporary dipole. |
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Functional Group Hydroxyl |
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Functional Group Carbonyl |
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Functional Group Carboxyl |
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Functional Group Sulfhydryl |
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Functional Group Phosphate |
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Interactions of non-polar substances. |
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Polymers that are composed of multiple monomers. |
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Synthesis of polymers by the linkage of a monomer and a polymer (a water molecule is lost). |
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Breakdown of polymers by adding a water molecule to break a bond. |
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Macromolecule composed of amino acids. |
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[image]
Characterized by the properties of the R group. |
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Are hydrophobic. End up at core of protein and effect how the protein folds. Also prevent the protein from unfolding. |
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Are hydrophilic. The amino acid cysteine contains a sulfhydral group (can react with other sulfhydral groups to from a disulphide bond). |
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Definition
5 amino acids whose R group can become charges at pH 7. |
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Organizational Levels of Polypeptide Folding |
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Definition
Primary: Chain/sequence of amino acids.
Secondary: Form alpha-helix and beta-sheets.
Tertiary: Final shape.
Quarternary: Two or more tertiary polypeptides joined together to form a functional protein. |
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Definition
Amino acids that are linked together by peptide bonds. The R groups on the amino acids dictate how the protein will fold. |
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Forms of Functional Proteins |
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Definition
Fibrous Proteins: Give shape and structure.
Globular Proteins: Used for chemical interactions. |
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When a protein loses its function due to unfolding or shape change. Heat/pH stresses can denature proteins. |
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Definition
Monosaccharides: Individual simple sugars.
Disaccharides: Pairs of monosaccharides.
Polysaccharides: Chains of monosaccharides.
All have the formula (CH2O)n |
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Are named based on number of carbons. Pentoses and hexoses can form ring structures in water. These ring structures will cycle between there two isomers. alpha-glucose has the hydroxyl group pointing down. beta-glucose has the hydroxyl group pointing up. |
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Two monosaccharides that are linked through glycosidic (links between glucose molecules) bonds. Water is removes to form bond. |
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Definition
Starch: Polymer of alpha-glucose (bonds are easy to break and polymer is good for storage).
Cellulose: Polymer of beta-glucose (bonds are very stable and polymer is good for structure).
Glycogen: Identicle to starch except it has multiple branches. |
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Definition
Macromolecules that a devided into: Fatty acids, fats, phospholipids, and steroids.
All lipids are hydrophobic and most are not polymers. |
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Definition
Formula: nC + nH + 2O
Saturated: Contain the maximum amount of hydrogens (pack together tightly and are solid at room temperature).
Unsaturated: have carbon-carbon double bonds (do not pack together tightly and tend to be liquid at room temperature). |
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Are made up of three fatty acids plus a glycerol. Glycerol forms ester bonds with the fatty acids via a condensation reaction. Are good for storgae but have no function. |
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Amphipathic molecules that have a hydrophilic phosphate head and a hydrophobic fatty acid tail. |
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Have a four ring structure and are made from cholesteral. |
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Macromolecules that are split into the double stranded deoxyribonucleic acid (DNA), and the single stranded Ribonucleic acid (RNA). Are polymers of nucleotides. Nucleic acids have a 3' end (sugar) and a 5' end (phosphate). |
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Definition
Contain three parts.
Phosphate group.
Sugar: Deoxyribose in DNA and Ribose in RNA.
Nitrogenous base (nucleoside): Split between the single ring pyrimidines (cytosine, thymine and uracil) and the double ring purines (adenin and guanine). |
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Combinations of two or more macromolecules.
Glycoproteins: sugar + protein.
Proteoglycans: sugar + protein.
Lipoproteins: Lipid + protein. |
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