importance of proteins
associated with strength and muscle
important for wound healing
Have functional and structural cells
Examples of proteins as working molecules
enzymes
antibodies
transport vehicles
hormones
cellular pumps
oxygen carriers
proteins for structure
tendons
ligaments
scars
fibres of muscles
cores of bone and teeth
filaments of hair
nails
Function of side chains
make amino acids differ in
- size
- shape
- electrical charge
impact folding and determine the molecules shapes and behaviours
essential amino acids
ones that cannot be synthesized within the body
Used by the body to make proteins
what other ways can our body make AA (nonessential ones)
from fragments of carbs or fat to form the backbone
and nitrogen from other soruces
Essential amino acids
MILK For The Very Hundreth Win
Methionine
Isoleucine
Leucine
Lysine
Phenylalanine
Threonine
Valine
Tryptophan
Conditionally indispensable essential amino acid
an AA that is normally nonessential
but when the needs are exceeded by the bodys ability to produce it it is needed from the diet
ex. Tyrosine from phenylalanine
Recycling amino acids
The body can make AA but also breaks fown protein to reuse them - from food and the body
the body only has a tiny AA pool to allow for protein molecules to be built
These AA can also be used for energy when needed
AA for energy
tissues can break down their own proteins in times of energy need
the most dispensable proteins are used first (from the blood and muscle)
- structural proteins for organs are guarded until situation is dire
How does a peptide bond form
condensation reaction
How big are proteins
several dozen to 1000 AA long
secondary structure (polypeptide shapes)
the interaction of the AA with eachother - twisting into a helix or folding into a pleated sheet
For strength and stability
Tertiary structure (polypeptide tangles)
the long poly peptide chains twist and fold into a variety of shapes
The attraction and repelling of side chains helps shape the protein
- hydrophilic = near surface
- hydrophobic = towards the middle
Disulphide bridges help determine structure as well
Quaternary structure
interactions between 2/+ polypeptides
they work tg in lg complexes
Proteins perform different tasks depending on their shape. Ex.
Globular = water soluble - in blood
Hollow balls = carry and store materials in their interior
Long = structure - tendons
Collagen
the protein of connective tissue
- acts like the glue between cells
- tendons, ligaments
The foundation for bones and teeth
Sickle cell disease (AA)
variation in AA sequence resulting in abnormal hemoglobin
Valine replaced by glutamic acid
- alters proteins ability to carry oxygen
Results in crescent shaped cells
- abnormal blood clotting, strokes, pain, infections
Denaturation of a protein
the irreversible change in a proteins shape
Caused by heat, acids, bases, alcohols
Important during digestion allowing for enzymes to interact with peptide bonds and cleave them
Protein digestions - overall
so proteins that are eaten must be broken down and absorbed
then the AA can be arranged into specific human body proteins
Protein digestion - mouth
Protein is crushed by chewing
Moistened with saliva
Protein digestion - stomach
acid helps denature proteins so that pepsin can attack peptide bonds
- cleaves polypeptides
Protein digestion - sm Intestine
receives sm denatured pieces of protein
- Most are poly peptides
- few are single AA
Alkaline juices from the pancreas neutralize stomach acid, allowing for protease within the sm intestine to break down proteins
= leaving di, tripeptides and single AA
Protein absorption - sm intestine
the sm intestine can absorb single AA
For any AA that couldn’t be made single by protease, the enzymes on the villi of the sm intestine finish digesting turning them into single so that they can be absorbed
Some are even absorbed as di or tri but split before being released into the blood