Chapter 7 - Protein Flashcards
protein
very large molecules composed of one or more chains of amino acids
molecules critical for muscle+bone structure, most biochemical reactions
4 different types: primary, secondary, tertiary, and quaternary
amino acids
very small molecules, building blocks of proteins
dipeptides, tripeptides, and polypeptides
hundreds of amino acids are found in nature, but only 20 are used by the human body
dipeptide
peptide composed of 2 amino acids
tripeptides
peptide composed of 3 amino acids
titin
A giant structural protein in the human body that helps provide structure to sarcomeres (the basic contractile unit of muscle fiber) in muscle tissue.
27,000 amino acids - one of the largest and most complex
how many structures of proteins are there?
4
primary, secondary, tertiary, and quaternary
protein structure
primary structure
the order of amino acids in peptide molecule
protein structure
secondary structure
The primary shape of a protein, usually classified as a
1. beta-sheet, or
2. alpha-helix.
protein structure
tertiary structure
The full, three-dimensional structure of a single chain of amino acids
protein structure
quaternary structure
The structure when two or more tertiary structures interact
types of protein
- fibrous
- globular
- membrane
protein type
fibrous proteins
These proteins form muscle fibers, tendons, connective tissue, and bones.
- collagen
- titin
- elastin
- myosin
- actin
protein type
globular proteins
These proteins are water-soluble, shaped like a globe or sphere and act as transport proteins, enzymes, and hormones
- hemoglobin
- albumin
- fibrin
- immunoglobulin A
- myoglobin
- insulin
protein type
membrane proteins
integral component of cell membranes
found in all cells and separates the interior of the cell from the outside environment
signaling proteins:
1. integral
2. peripheral
3. lipid-anchored
essential amino acids
cannot be synthesized by the body, must be consumed through the diet
1. histidine
2. lysine
3. methionine
4. phenylalanine
5. thrreonine
6. tryptophan
7. branched-chain amino acids
8. isoleucine
9. leucine
10. valine
p i t t h m b l l v
non-essential amino acids
Amino acids that the human body is capable of manufacturing to a large enough degree that they are not required to be consumed through the diet
1. alanine
2. asparagine
3. aspartic acid
4. glutamic acid
5. serine
6. Arginine
7. Cysteine
8. Glutamine
9. Glycine
10. Proline
11. Tyrosine
c a a a a g g g s t p
4 steps of protein metabolism
- chewing
- stomach acid
- small intestine
- bloodstream
factors affecting protein absorption
internal factors: related to the human body
external factors: related to the protein source itself
factors affecting protein absorption
external factors
- state of protein (liquid or solid)
- cooked or not
- complexity of the protein type/structure
- whether it is consumed in isolation
external absorption factors
liquid proteins
Liquid protein sources (e.g., whey protein or dairy) are often more efficiently absorbed when compared to solid sources
This is true in part because liquid proteins require little to no mechanical digestion and are more easily digested enzymatically by peptidases in the stomach
external absorption factors
food processing
around 90% of cooked egg protein is absorbed while only ~50% of raw egg protein is absorbed
external absorption factors
complexity of protein structure
proteins that contain smaller peptides, such as di- or tripeptides, are often absorbed slightly faster than proteins that have longer peptide chains
Whey protein is a good example of this, especially in the context of sports nutrition. There is some evidence that consuming a hydrolyzed whey protein, which is enzymatically pre-digested, is absorbed slightly faster than a fully intact whey protein
external absorption factors
consuming protein in isolation
consuming protein in isolation appears to be more beneficial for acutely maximizing absorption when compared to mixed meals
There are some tools that the Sports Nutrition Coach can use to help determine how digestible a protein source is and how much that protein source contributes to the free amino acid pool
internal absorption factors
stomach enzymes
the amount of peptidases (peptide digesting enzymes) present in the gastrointestinal tract varies from person to person
the less peptidases present, the less efficient someone will digest and absorb protein
internal absorption factors
stomach acid
stomach acid also affects protein digestion and absorption
individuals with less stomach acid often absorb less of the protein they consume
internal absorption factors
volume of protein consumed
the efficiency of digestion and absorption decreases as the volume and amount of protein increases
For example, if someone consumes ~10 grams of protein, they will absorb a higher percentage of those 10 grams than they would if they were to consume ~100 grams of protein
Digestion, Absorption, and the Athlete
The digestive and absorptive properties of various proteins can have important impacts on athletes
For example, the digestive properties of proteins can influence the anabolic response to protein both during exercise and at rest. These proteins are often classified as fast or slow based on digestion and absorption The majority of research into fast and slow protein compares whey, casein, and soy (the most commonly consumed isolated protein). Whey and soy are considered to be fast proteins, whereas casein is slow. Another factor to consider when choosing the type of protein to consume is the amino acid content, specifically leucine. This amino acid acts as a signaling molecule that stimulates protein synthetic pathways such as mTOR.
Whey protein contains more leucine than casein or soy; however, supplementation can often contain additional leucine, which promotes anabolic response post-exercise