Digestion
Once amino acids have entered the blood stream they travel to this organ that regulates it’s distribution to the rest of the body
The liver
This occurs when the rate of protein synthesis exceeds the rate of breakdown
Positive protein balance
note: this is typically seen during periods of growth, such as infancy, childhood, adolescence, and pregnancy. It also occurs during periods of recovery from illness or injury.
note: the opposite is negative protein balance which is where protein breakdown exceeds protein synthesis.
This occurs when protein can’t properly balance fluids and fluids leak from the blood into interstitial space.
Edema
note: edema is palpable swelling caused by the expansion of fluid in interstitial space
typically proteins attract fluids and keep them in the blood vessels pulling fluid in with every heart beat but with a limited amount of protein the pressure of blood against capillaries forces fluid out.
The ratio of g/kg a person should consume to maintain muscle mass.
0.8g protein /kg body weight
The building blocks of protein
Amino acids
The process of unfolding proteins and exposing peptide bonds
Denature
note: when we eat protein, it is denatured in the stomach due to the acidic environment, primarily because of stomach hydrochloric acid (HCl), after a protein is denatured and the peptide bonds are exposed, enzymes can start breaking those bonds
This process ensures the concentration of amino acids are maintained within a narrow range in the body
Active transport
note: Active transport systems are specific and can recognize amino acids based on their structures. Different amino acid transporters exist for different amino acids, making sure each amino acid is taken as needed. The activity of these transporters are regulated by dietary intake, hormonal signals, and metabolic demands. Active transport also helps maintain intracellular concentrations of amino acids and prev excess accumulation in extra cellular space by removing excess from the bloodstream and maintaining homeostasis
These proteins defend the body by recognizing and neutralizing foreign invaders
Antibodies
What can impact protein needs?
Age, athletic vs. sedentary lifestyle, illness, injury, pregnancy, lactation.
the protein structure containing one or more amino acid chain
Quaternary structure
The Enzyme who’s inactive form is secreted by chief cells in stomach that is activated by the acidic environment, used to break the peptide bonds associated with specific amino acids.
Pepsin
note: the inactive form is pepsinogen, pepsin breaks down large protein molecules into smaller peptide fragments through hydrolysis, primarily breaking peptide bonds adjacent to certain amino acids like phenylalanine, tyrosine, and leucine.
When Active Transport is used to pump amino acids from an area of low concentration to an area of high concentration
Active transport Against concentration gradient
note this allows cells to accumulate amino acids even when the extra cellular concentration is low
These have a stimulatory effect on tissues and help regulate biological processes such as muscle growth, hunger, heart rate, and menstrual cycles
Hormones
These proteins contain insufficient amounts of one or more of the 9 essential amino acids
Incomplete proteins
note: the 9 essential amino acids cannot be synthesized within the body and must be provided by diet.
This protein structure is categorized by the folding of polypeptide chains into alpha helix or beta pleated sheets
Secondary structure
The Hormone that stimulates the pancreas to release its enzymes into the sm. Intestine
Cholecystokinin (CCK)
Note: the acidic chyme of the stomach entering the sm. Intestine is what triggers CCK’s release.
This type of protein deficiency is seen with an overall calorie deficiency including protein carbs and fat and is characterized by severe wasting of muscle and fat giving a ”skin and bones” appearance
Marasmus
These speed up chemical reactions aiding in digestion and metabolism
Enzymes
This is the amino acid found in the shortest supply of an incomplete protein
Limiting amino acid
this part of an amino acid determines the function of a protein
The side chain
note if it is polar it will interact with water soluble, nonpolar with fats, if it is negatively charged it will be acidic, positive basic.
The main protein-digesting enzymes released from the pancreas that breaks the peptide fragments from the stomach into smaller peptides and individual amino acids.
Trypsin and Chymotrypsin
note: these proteases help form tripeptides, dipeptides, and amino acids
This form of malnutrition is caused by severe deficiency in dietary protein intake but with adequate caloric intake. Those who suffer from this often exhibit edema in the abdomen, face, hands, and feet. They also can have skin lesions, hair changes, irritability, and anorexia
Kwashiorkor
note: kwashiorkor is typically seen in children who are weaned from breast milk to a low-protein diet. It also impairs immune function due to a decrease in the synthesis of antibodies and white blood cells, leaving those with this condition susceptible to infection. It also harms the metabolism causing impaired growth and metabolic abnormalities. For this reason it is the most dangerous form of protein deficiency.
The 7 functions of protein
Form hormones, antibodies, and enzymes, balance fluid and pH in the body, provide energy, and transport substances such as oxygen, fats, and nutrients.
What are conditional essential amino acids?
Conditionally essential amino acids are amino acids outside the 9 essential that become essential during times of physical stress and healing
The structure caused by side chain interactions forming 3-D folding patterns
Tertiary structure