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PROTEINS

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Terms in this set (21)

  • Primary Structure

    covalent bonds

  • Electrostatic Interactions

    aka ionic Salt Bridges

    between acidic/ base side chains, amino/ carboxyl termini, acidic/ base side chains and N/C termini

    SECONDARY, TERTIARY , QUANTARY STRUCTURE

  • Hydrogen Bonds

    backbone of SECONDARY STRUCUTRE

  • Van der Waals Forces

    between all atoms

  • Hydrophobic Effect

    exclusion of water by nonpolar groups cause proteins to fold

    TERTIARY/ QUANTARY STRUCUTRE

  • Glycoproteins

    covalently bound to carbs (glucose/ sugar)

  • Lipoproteins

    convalently bound to lipids

  • Metalloproteins

    mental ions for stablization/ catalyst

  • Phosphoproteins

    covalenly bound to P groups used to activate/ deactivate a protein or provide binding sites for protein attachment

  • Hemoproteins

    contains heme groups/ porphyrin rings

  • Nucleoproteins

    contain ribonucleic acids (protein synth)

  • Nonoploar amino acids

    look for CH chains/ groups

  • Neutral Polar

    look for OH , SH, O 2x bond to C

  • Steroisomers

    atoms bonded in same order but w/ dif arrangments

  • Enatiomers

    mirrow images of steroisomers

    each isomer has a C atom bonded to four different functional (R) groups

  • Didsteroisomers

    steroisomers that aren't mirror images

  • N- terminal

    NH2 amino group

  • C-terminal

    COOH carboxyl group

  • nonpolar

    hydrophobic

    van der waals interactions

  • polar

    hydrophilic

    h-bonds between backbone amide groups (stablize secondary strucutre)

  • Chaperones

    proteins that help other proteins fold