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45 Cards in this Set
- Front
- Back
- 3rd side (hint)
Essential amino acid (p) |
Phenylalanine |
Associated with a genetic disease requiring special protein supplements. |
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Essential amino acid (m) |
Methionine |
The first amino acid on any chain of protein in the body. |
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Essential amino acid (T) |
Tryptophan |
People talk about it in relation to thanksgiving turkey. |
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Essential amino acid (V) |
Valine |
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Essential amino acid (h) |
Hiatidine |
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Essential amino acid (I) |
Isoleucine |
Associated with a different amino acid. |
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Essential amino acid (L) |
Leucine |
Offen claimed to be low in vegans. |
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Essential amino acid (Ly) |
Lysine |
Often claimed to be the reason why vegans can't build muscle. |
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Essential amino acid (th) |
Threonine |
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Non-essential amino acid (Al) |
Alanine |
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Non-essential amino acid (AA) |
Aspartic Acid |
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Non-essential amino acid (as) |
Asparagine |
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Non-essential amino acid (g) |
Glutamic acid |
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Non-essential amino acid (s) |
Serine |
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Conditionally essential amino acid (A) |
Arginine |
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Conditionally essential amino acid (c) |
Cysteine |
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Conditionally essential amino acid (g) |
Glutamine |
People take this for their joints. |
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Conditionally essential amino acid (gl) |
Glycine |
Found in collagen |
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Conditionally essential amino acid (p) |
Proline |
Found in collagen |
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Conditionally essential amino acid (T) |
Tyrosine |
Has to be supplemented into vegan cat food. |
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Four parts of an amino acid |
1. Central carbon 2. Acid group 3. Amino group 4. R group |
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Transamination |
The transferring of an amino group from one amino acid to a different one. |
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Deamination |
The removal of an amino group when it doesn't get attached to a different carbon skeleton. |
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Limiting amino acid |
The amino acid in the smallest supply. Limits the proteins the body can make. |
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Bonds used to link amino acids |
Peptide bonds |
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Primary structure of an amino acid |
Sequence of amino acids. This determines the protein's shape. |
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Secondary structure of proteins |
The shape that the amino acid chain twists into, formed by weak bonds between the amino acids. |
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Tertiary structure of proteins |
Three dimensional folding of twisted chains, overall shape. |
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Quarter art structure of proteins |
2 or more peptides interacting. |
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Nitrogen Balence |
Method to determine protein need. |
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Negative nitrogen balence |
A person is eating less protein than they need. Can lead to diseases that increase protein breakdown. |
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Positive protein balence |
Protein intake greater than losses Occurs durring growth, recovery and intense athletic training. |
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RDA for protein |
0.8 g per kg bodyweight |
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AMDR for protien |
10% - 35% of calories |
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Stomach enzyme for protien breakdown |
Pepsin |
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Hormones secreted when protein exits the stomach |
Secretin Cholecystokinin |
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Enzymes for protein digestion |
Trypsin Chymotrypsin Carboxypeptidase |
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Peptide absorption |
1. Active absorption absorption into cells 2. Continue to be digested 3. Transformed in the liver |
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Uses for proteins |
1. Protein synthesis 2. Energy needs 3. Conversion to fat or carbs |
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Function of albumin and globulin |
These proteins maintain fluid balance in the blood and can drop when people do not eat enough protein. |
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How do proteins help acid-base balance? |
They pump ions into and out of cells by attracting positively charged hydrogen ions. |
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How do proteins contribute to immune function? |
Antibodies are proteins and without enough of them your body's ability to fight infection is reduced. |
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Retinal-binding protein |
Protein that carries vitamin A |
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Transferin and ferritin |
Proteins that carry and store iron |
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Ceruloplasmin |
Protein that carries copper. |
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