 The structure of proteins

1. Protein 4 cal/gm-contains nitrogen

2. Amino Acids-single units-make protein
Carbon atom with amine group + acid group
Side chain-determine role of protein
Amino acid = 1
Dipeptide=2
Trpeptide=3
Oligopeptide=4-9
Polypeptide= >10
 Amino acids
1. 20 amino acids-total
2. 9 essential amino acids-from diet
Conditionally essential
Normally nonessential
Under condiciotn becomes essesntial
PKU-tyrosine
Becomes essential
3. 11 non essential amino acids
Recycling-breakdown old protein
Reuse amino acids
Priority system-most critical are used last
Blood, muscle, and hair is given first
Heart, liver, kidney’s-saved until needed
 How do amino acids build proteins?
1. Peptide bonds-very strong bond
Broke in acidic condition-stomach (Ph2)
Links one amino acids to another
2. Strands of amino acids not straight
Coils and folds
3. Side chain electrical charge
Positive, negative, or neutrall
 Variety of proteins
1. Protein shape-performance and tasks
2. Single cell contain 10,000 proteins
Worker proteins
Insulin, antibodies, hemoglobin, enzymes
Enzyme-protein catalyst
Causes a reaction without itself being altered
HCL in the stomach
Builder proteins
Hair, skin, nails, cells, and collagen
Collagen-protein from which connective tissue is made
Most abundant protein in your body
 Protein strands
1. Inherited amino acid sequences
Amino acids order of placement
Alterations to sequence-genetic
Sickle cell disease
Valine instead of glutamine
Cresent shaped blood cells
Not carry oxygen
2. Nutrients and gene expression
Vitamin C, folic acid, B6
 Denaturation of proteins
1. Denature
Irreversible change to the protein structure
Acids-stomach
Bases-bicarb
Heat-cooking
Alcohol
Salts of heavy metals
Mercury silver
 Protein digestion
1. Stomach-acidic-HCL
2. Denatures protein in food
Uncoil protein-cleave peptide bond
Stomach protected by mucus layer
3. What to do if mercury is consumed
Drink milk
Milk protein denatured not body protein
Vomit altered milk