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33 Cards in this Set
- Front
- Back
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covalent chemical bonds
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shared electrons
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dipole
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non-covalent bond; weaker than covalent; polar bond with partial positive and partial negative character
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hydrogen bonds
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share protons; water H bonds with self and other molecules
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ionic interactions
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also called salt bridges; attraction between positive and negative charges
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hydrophobic interactions
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result in increased entropy as water is excluded from between hydrophobic molecules and can move more freely
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van der Waals forces
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transient dipolar forces
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acid
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proton donor
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base
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proton acceptor
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Henderson-Hasselbalch equation
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pH = pKa + log [A-]/[HA]
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nucleotides
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make up DNA, RNA and important molecules like ATP
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amino acids
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linked together to make proteins; provide structure and function to cell
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lipids
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form bilayers to separate cell from environment and for energy storage
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sugars
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metabolic fuel; building blocks for DNA and RNA; glycoproteins; mucopolysaccharides
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functional groups
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what is responsible for a biological molecule's specific properties
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alpha carbon
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carbon atom that links the amno and carboxyl groups that make up an amino acid
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R group
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side chains in the position of the H on the alpha carbon of amino acids; what makes each amino acid unique
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aliphatic, uncharged, hydrophobic amino acids
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Glycine (Gly), Alanine (Ala), Valine (Val), Leucine (Leu), Isoleucine (Ile)
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hydroxyl, uncharged, hydrophilic amino acids
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Serine (Ser), Threonine (Thr)
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Basic, positive (His is either pos or zero) amino acids
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Lysine (Lys), Arginine (Arg), Histidine (His)
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acidic, negative or uncharged amino acids
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Aspartate (Asp) - negative, Aspargine (Asn) - uncharged, Glutamate (Glu) - negative, Glutamine (Gln) - uncharged
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aromatic, hydrophobic, absorbs UV light amino acids
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Phenylalanine (Phe), Tyrosine (Tyr), Tryptohphan (Trp)
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sulfur-containing amino acids
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Cysteine (Cys), Methionine (Met)
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Imino (secondary)
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Proline (Pro)
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isoelectic point
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pI = Ph of zero net charge
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pKa for alpha and side carboxyls (Asp, Glu)
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4.0
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pKa for alpha-amino
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8.0
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pKa for sulfhydryl, -SH (Cys)
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8.5
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pKa imidazole, -NH (His)
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6.5
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pKa phenol, -OH (Tyr)
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10.0
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E-amino, -N+H3 (Lys)
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10.5
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guanidinium (Arg)
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12.0
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ornithine
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alpha-amino, alpha-carboxylic L-amino acid; one methyl group shorter than Lys; not coded for by DNA; not used to make proteins; result from metabolic process
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hydrophobicity
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important for protein folding; more hydrophobic proteins will be located on the interior of the protein
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