Term
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Definition
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Term
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Definition
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Term
| Formation of α-helix and β-sheets |
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Definition
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Term
| 3-dimensional shape of protein |
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Definition
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Term
| More than one polypeptide (dimers, oligomers) |
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Definition
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Term
| ___ amino acids found in proteins |
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Definition
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Term
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Definition
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Term
| body does not synthesize ______ amino acids |
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Definition
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Term
| ____ non-essential amino acids |
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Definition
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Term
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Definition
| carboxy group, amino group, and H off of center carbon |
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Term
| each of the 20 AA's have a ______ on center carbon |
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Definition
| unique side chain (R- group) |
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Term
| depending upon the unique side chain, the AAs are classified as: |
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Definition
| Acidic, basic, polar, non-polar (very hydrophobic) |
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Term
| Have carboxylic acid group in side chain |
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Definition
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Term
| Asp and Glu belong to what classification |
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Definition
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Term
| Lys - Arg- and His belong to what classification |
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Definition
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Term
| Have amines in side chain |
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Definition
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Term
| Amides or hydroxyl groups in side chains |
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Definition
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Term
| Asn, Gln, Ser, Thr, Tyr belong to what classification |
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Definition
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Term
| contains -OH group that can be phosphorylated |
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Definition
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Term
| Hydrocarbons in side chain |
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Definition
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Term
| Ala, Gly, Leu, Lleu, Pro, Phe, Met, Trp, Cys, Val belong to what classification |
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Definition
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Term
| contains -SH that can form disulfide bonds |
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Definition
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Term
| Cells do not synthesize these amino acids, therefore it is essential that you get them from diet |
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Definition
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Term
| The 8 essential amino acids |
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Definition
| Threonine, Methionine, Lysine, Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan |
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Term
| amino acids linked together through peptide bond via dehydration synthesis |
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Definition
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Term
| amino acids linked together through peptide bond via _____ (primary structure) |
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Definition
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Term
| NH3(+)-CHR-CONH-CHR-COO(-) |
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Definition
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Term
| In a primary structure, NH(+)-CHR-_____-CHR-COO(-) |
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Definition
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Term
| 2-100s of amino acids make up a _______ |
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Definition
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Term
| 2-100S of amino acids make up a polypeptide in a _____ structure |
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Definition
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Term
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Definition
| α-helix (secondary structure) |
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Term
| due to hydrogen bonding between C=O and N-H of two amino acids |
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Definition
| α-helix and β-sheets (secondary structure) |
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Term
| hydrogen bonding within polypeptide backbone (does not involve the unique side groups) |
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Definition
| α-helix and β-sheets (secondary structure) |
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Term
| zig-zagging of amino acids |
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Definition
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Term
| very stable and rigid structures |
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Definition
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Term
| Formation of these structures do not involve unique side chains, therefore they do not require a unique amino acid sequence to form |
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Definition
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Term
| Folded polypeptide strand into three dimensional shape |
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Definition
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Term
| no two proteins will have the same ____ structure |
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Definition
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Term
| determined by unique amino acid sequence |
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Definition
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Term
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Definition
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Term
| types of bonds that will stabilize tertiary structure |
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Definition
| hydrophobic interaction, hydrogen bond, ionic bond, van der waals attractions, and disulfide bridge/bond |
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Term
| interactions formed between molecules due to nonpolar tendencies |
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Definition
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Term
| dimers and obigomers are examples of |
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Definition
| more than one polypeptide chain |
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Term
| each polypeptide chain is called a _____ |
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Definition
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Term
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Definition
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Term
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Definition
| homodimers and heterodimers |
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Term
| protein containing more than two polypeptide chains |
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Definition
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Term
| types of bonds stablizing quaternary structure |
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Definition
| hydrophobic interaction, hydrogen bond, ionic bond, van der walls attraction, disulfide bridge |
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Term
| Not all proteins have _________ structure |
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Definition
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