PROTEIN NG MAMA MO

Subdecks (2)

Cards (202)

  • Protein
    A naturally-occurring, unbranched polymer in which the monomer units are amino acids
  • Proteins are the most abundant molecules in cells after water - account for about 15% of a cell's overall mass
  • Amino acid

    An organic compound that contains both an amino (-NH2) and carboxyl (-COOH) groups attached to same carbon atom
  • Elements found in proteins
    • Carbon (C)
    • Hydrogen (H)
    • Nitrogen (N)
    • Oxygen (O)
    • Sulfur (S)
    • Iron (Fe)
    • Phosphorus (P)
    • Other metals
  • The average nitrogen content of proteins is 15.4% by mass
  • Standard amino acids
    • Non-polar
    • Polar neutral
    • Polar acidic
    • Polar basic
  • Non-polar amino acids

    Hydrophobic (water-fearing, insoluble in water)
  • Polar neutral amino acids

    Contain polar but neutral side chains
  • Polar acidic amino acids

    Contain carboxyl group as part of the side chains
  • Polar basic amino acids

    Contain amino group as part of the side chain
  • Amino acid nomenclature

    Common names, three letter abbreviations, one letter symbols
  • Chirality
    19 of the 20 standard amino acids contain a chiral center and exist in left and right handed forms (L and D isomers)
  • The amino acids found in nature as well as in proteins are L isomers
  • Zwitterion
    An ion with + (positive) and - (negative) charges on the same molecule with a net zero charge
  • Isoelectric point (pI)
    pH at which the concentration of Zwitterion is maximum - net charge is zero
  • Cysteine
    The only standard amino acid with a sulfhydryl group (-SH)
  • Cystine
    Two cysteine residues linked via a covalent disulfide bond
  • Peptide
    An unbranched chain of covalently-linked amino acids
  • Types of peptides
    • Dipeptide
    • Oligopeptide
    • Polypeptide
  • Peptide nomenclature
    1. terminal amino acid keeps full name, other amino acids have -yl suffix
  • Isomeric peptides
    Peptides with same amino acids but in different order are different molecules
  • Biochemically important small peptides
    • Hormones
    • Neurotransmitters
    • Antioxidants
  • Oxytocin and vasopressin
    Small peptide hormones produced by the pituitary gland
  • Enkephalins
    Small peptide neurotransmitters that help reduce pain
  • Glutathione
    A tripeptide antioxidant that protects cells from oxidizing agents
  • Protein
    A peptide in which at least 40 amino acid residues are present
  • Protein classification by chemical composition
    • Simple proteins
    • Conjugated proteins
  • Primary structure of proteins

    The order in which amino acids are linked together
  • Frederick Sanger sequenced and determined the primary structure for the first protein - Insulin
  • Proteins of the same organism always have the same amino acid sequence
  • Insulin from different sources (pigs, cows, sheep, humans) are similar but have some differences
  • Human insulin is now produced from genetically engineered organisms
  • Primary Structure
    The order in which amino acids are linked together in a protein
  • Every protein has its own unique amino acid sequence
  • Frederick Sanger (1953)
    Sequenced and determined the primary structure for the first protein - Insulin
  • Proteins of the same organism always have the same sequence (cows, pigs, etc.)
  • Different sources: Insulin from pigs, cows, sheep, humans are similar
  • Some differences in insulin may show some reaction over time
  • Now human insulin is produced from genetically engineered bacteria
  • Secondary Structure
    Arrangement of atoms of backbone in space