GCU BIO 319: LATEST A+ QUESTIONS AND ANSWERS
GUIDE FOR ULTIMATE SUCCESS
The nine essential amino acids are
histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine
The chemical structures of amino acids
Amino Group, Carboxyl Group, Side Chain
The Chemical Structure Of Protein
Protein Digestion
-Protein foods denatured by stomach acids (HCl)
-Enzymes (Chymotrypsin, trypsin, pepsin and HCl (acid)) from stomach, pancreas, and small intestine
digest proteins
-Free amino acids are formed
Where is 90% of protein digested?
Small Intestine
Protein absorption
-Amino acids absorbed by villi
-Delivered to cells via blood
-Amino acids rebuilt as needed into new protein in the cells.
Describe the process of protein synthesis
transcription and translation. Transcription takes the information encoded in DNA and encodes it into
mRNA, which heads out of the cell's nucleus and into the cytoplasm. During translation, the mRNA
works with a ribosome and tRNA to synthesize proteins.
Describe the process of protein transamination
Transfer amine group (NH2) from essential amino acid to a different acid group and R group.
Used to make nonessential amino acids
Describe the process of protein denaturation
Proteins uncoil and lose their shape
-Protein function is lost (shape = function)
-Causes:
Temperature pH Enzymes Alcohol
Amino Acid kinds
Dipeptide
Tripeptide
, Polypeptide
Protein
-Dipeptide: 2 amino acids
-Tripeptide: 3 amino acids
-Polypeptide: more than 3 amino acids
-Protein: 70 or more amino acids
Average protein ~200 amino acids!
Describe the process of protein deamination
deamination occurs when an excess in protein is consumed, resulting in the removal of an amine group,
which is then converted into ammonia and expelled via urination. This deamination process allows the
body to convert excess amino acids into usable by-products.
Major Functions Of protein
1. Growth and maintenance: building blocks of muscle, blood and skin
2. Body processes: Hormones(messenger molecules that tell
something to happen - insulin, glucagon), enzymes(digestion, DNA synthesis), Antibodies(large proteins
that are produced by your immune system to fight viruses), transport proteins (brining important
substances in and out of your cells, lipoproteins)
3. Energy
4. Fluid and Electrolyte balance: proteins attract water and keeps it where it is supposed to be
Diatary recommendations for protein intake
1. RDA-0.8gramsperkghealthybody weight
2. AMDR-10-35%totalkcals
Excessive intake of protein can result in
obesity
High cholesterol and heart disease
Contribution to bone loss
Kidney disease
Protein deficiencies
Kwashiorkor (Protein Malnutrition)
Disease resulting from low protein intake
Occurs often when child taken off breast milk and fed starchy liquid
Usually develops very rapidly Symptoms:
Some weight loss and muscle wasting Retarded growth and development Edema: swollen bellyFatty
degeneration of the liver
Loss of appetite, sadness, irritability, apathy Skin problems and hair lossDeath
Protein deficiencies
GUIDE FOR ULTIMATE SUCCESS
The nine essential amino acids are
histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine
The chemical structures of amino acids
Amino Group, Carboxyl Group, Side Chain
The Chemical Structure Of Protein
Protein Digestion
-Protein foods denatured by stomach acids (HCl)
-Enzymes (Chymotrypsin, trypsin, pepsin and HCl (acid)) from stomach, pancreas, and small intestine
digest proteins
-Free amino acids are formed
Where is 90% of protein digested?
Small Intestine
Protein absorption
-Amino acids absorbed by villi
-Delivered to cells via blood
-Amino acids rebuilt as needed into new protein in the cells.
Describe the process of protein synthesis
transcription and translation. Transcription takes the information encoded in DNA and encodes it into
mRNA, which heads out of the cell's nucleus and into the cytoplasm. During translation, the mRNA
works with a ribosome and tRNA to synthesize proteins.
Describe the process of protein transamination
Transfer amine group (NH2) from essential amino acid to a different acid group and R group.
Used to make nonessential amino acids
Describe the process of protein denaturation
Proteins uncoil and lose their shape
-Protein function is lost (shape = function)
-Causes:
Temperature pH Enzymes Alcohol
Amino Acid kinds
Dipeptide
Tripeptide
, Polypeptide
Protein
-Dipeptide: 2 amino acids
-Tripeptide: 3 amino acids
-Polypeptide: more than 3 amino acids
-Protein: 70 or more amino acids
Average protein ~200 amino acids!
Describe the process of protein deamination
deamination occurs when an excess in protein is consumed, resulting in the removal of an amine group,
which is then converted into ammonia and expelled via urination. This deamination process allows the
body to convert excess amino acids into usable by-products.
Major Functions Of protein
1. Growth and maintenance: building blocks of muscle, blood and skin
2. Body processes: Hormones(messenger molecules that tell
something to happen - insulin, glucagon), enzymes(digestion, DNA synthesis), Antibodies(large proteins
that are produced by your immune system to fight viruses), transport proteins (brining important
substances in and out of your cells, lipoproteins)
3. Energy
4. Fluid and Electrolyte balance: proteins attract water and keeps it where it is supposed to be
Diatary recommendations for protein intake
1. RDA-0.8gramsperkghealthybody weight
2. AMDR-10-35%totalkcals
Excessive intake of protein can result in
obesity
High cholesterol and heart disease
Contribution to bone loss
Kidney disease
Protein deficiencies
Kwashiorkor (Protein Malnutrition)
Disease resulting from low protein intake
Occurs often when child taken off breast milk and fed starchy liquid
Usually develops very rapidly Symptoms:
Some weight loss and muscle wasting Retarded growth and development Edema: swollen bellyFatty
degeneration of the liver
Loss of appetite, sadness, irritability, apathy Skin problems and hair lossDeath
Protein deficiencies
