Chapter 6: Protein Flashcards
Critical Roles in the body
- Structure material
-Growth, maintenance, and repair
-Energy Source - Critical functions ( enzymes, hormones , antibodies sacide base balance, transportes, blood clotting
RDA (Recommended Dietary Allowance)
AMDR (Acceptable Macronutrient Distribution Range)
RDA=0.8g/kg
AMDR 10%-35%
Amino Acid Structure
central carbon atom + amino group + acid group + hydrogen attach to carbon + a side chain
There are_ amino acids that differ by _
20 amino acids
Side chain
What link amino acids together and what connects
Peptide bonds. Acid group of one amino acid is joined with th amino group of other amino acid
2 amino acids
3 amino acids
Many amino acids
Dipeptides
Tripeptides
Polypeptides
There are _ essential amino acids and _ non-essential
9 and 11
Essential amino acid
HVPMTTILL
Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
Non essential amino acids
Alanine
Arginine
Asparagine
Asparatic acid
Cysteine
Glutamine acid
Glutamine
Glycine
Proline
Serine
Tyrosine
two steps for protein synthesis
transcription- nucleus; DNA is transcribe (produces) mRNA and then exported to cytoplasm
translation- cytoplasm (ribosome); amino acids are bonded together by peptide bonds to form protein
what’s protein folding
folding of amino acid chain into a particular shape and determines the protein’s function
To function properly, proteins must retain 3-dimensional shape
protein denaturation
change in3D shape by Caused by heat, light, pH (acidity/stomach/HCl), alcohol, or motion
Important in digestion
what denatures protein
HCl
eggs are a source of complete protein
TRUEEEEEEEEEE
What’s a complete protein
CONTAINS ALL THE 20 NATURAL OCCURING AMINO ACIDS
what is the other example of complete protein
WHEYYYY
describe the process of protein digestion and absorption
NO protein enzyme in the mouth
-mechanical digestion
stomach
acidic juices (HCl) denature protein
pepsin protein digestive enzyme
small intestine
pancreatic protease (di-tri-monopeptides) continues the process of protein breakdown
Mucosa space - pool of amino acids (and then circulatory space)
absorption of amino acids
What’s pepsin
protein digestive enzyme
protein turnover
relationship between protein synthesis and breakdown
protein breakdown rate exceed protein synthetic rate (similar to nitrogen balance)
body protein mass decrease and vice versa
amino acid pool is from both
body protein and food
what are the 3 fate of amino acid
Primary
Synthesize proteins in the body
Secondarily
Metabolized as a source of energy (amino acid)
Secondarily
Synthesized into glucose or fat (rarely)
The two last is if there’s a carbohydrate depletion
What’s RDA for protein
0.8 g/kg
what’s AMDR for protein
10%-35%
what’s the optimal intake for active individuals
1.2-1.7 g/kg
how are protein quality classified
Complete proteins
Contain all nine essential amino acids
Incomplete proteins
Lack one or more amino acids
Limiting amino acid
Complementary protein
Combining incomplete proteins
eg: rice and beans
what is the disease for protein deficiency
kwashiorkor (swollen belly from edema and fatty liver)
marasmus- skin and bones
