Chapter 6

Cards (40)

  • Protein Turnover: existing proteins are degraded into AAs for new proteins
  • Amino acid pool: AAs from food and cellular breakdown
  • Essential amino acids: 9, obtains from food
  • Nonessential: synthesized by body
  • Transamination: transfer amine group from an essential amino acid to a different acid group
  • Conditionally essential: non-essential becomes essential due to a condition or lakc of nutrients
  • Limiting amino acid: missing in the small supply, slows or halts protein synthesis
  • Incomplete protein (low quality): insufficient AAs, does not support growth or health
  • Complete protein (high quality): sufficient amounts of all 9 essentials, derived from animal sources, soy beans, and quinoa
  • Mutual supplementation: combine 2+ imcomplete protein sources to make a complete protein
  • Complementary proteins: 2 or more foods that contain the complete AA profile
  • RDA for Protein
    0.8g per kg of body weight
    during higher growth periods like developments theyre needed more
  • Protein AMDR: 10-35%
  • Most americans meet or exceed the RDA
  • Protein-energy malnutrition: disorder caused by inadequate protein and energy intake
  • Marasmus: inadequate energy, protein, and nutrient intake
  • Kwashiorkor: low protein intake
  • Vegetarianism: restricting diet to plant foods
  • ProteinsL large complex molecules found in all living tissues, dictated by DNA
  • What are proteins made of?
    20 amino acids
  • Proteins are long amino acids chains, peptide bonds hold these together
  • Gene expression: cells use genes to express proteins
  • Transcription: mRNA copies genetic information from the DNA in the nucleus
  • Translation: mRNA transcribed into an AA sequence at a ribosome
  • Primary protein structure: The sequence of amino acids in a polypeptide chain
  • Secondary protein structure: spiral shape or twisting of the AA chain
  • Tertiary Protein Structure: three dimensional sjape from hydrogen bonds and disulfide bridges. determines it's function
  • Quaternary protein structure: polypeptides bond to form larger proteins
  • Proteins: can be globular or fibrous
  • Protein denaturing: loose shape when exposed to heat, acid, base, heavy metals, or alcohol. Their function is lost forever.
  • Protein function loss
  • Nitrogen balance: determines proteins needs
  • Positive nitrogen balance: consuming more nitrogen than is excreted (growth, pregnancy, recovery from illness)
  • Negative nitrogen balance: excreting more nitrogen than taken. (starving, low-energy diet)
  • Bone health: higher intakes of animal and soy show to protect bones in middle-aged or older women
  • High protein intake may be beneficial in some populations
  • High protein diets can increase calcium excretion, this does not degrade bone structure
  • Kidney Disease: high protein diets can increase risk of kidney disease in diabetics. 2g of protein per kilo of body weight is safe for healthy people
  • Intaking more water with protein intake is reccomended
  • Elevated blood cholesterol increases risk of CVD, associated with protein diets. Recommended to limit sat. fats and replace with poly unsat. fats