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What proteins are made up of
Have an amino group, an acid, a hydrogen, carbon molecule, and a carbon side chain
Can also contain sulfur, phosphorus, or iron
How proteins are connected
Peptide bonds connect the acid end of one amino acid with the amino end of another
They are links that form a protein chain, which can be simple or very complex
Essential vs non-essential amino acids
Nonessential → can be made within the body
Essential → cannot be made in the body (must be obtained from foods)
How amino acids are held together
Held together by peptide bonds:
water cna hydrolyze a bond and break the amino acids apart (e.g. digestion)
Dehydration can make a bond (protein synthesis)
Organization of Proteins
Properties of amino acids (e.g. polar vs non-polar) create attractions between AA
causes folding, bending
Secondary and tertiary structure
Four Levels of Protein Structure: Primary Structure
Unique sequence of amino acids in a polypeptide
Linear organization
Four Levels of Protein Structure: Secondary Structure
Folding or coiling of the polypeptide
Includes the a helix and the B pleated sheet
Four Levels of Protein Structure: Tertiary Structure
3-D shape of a polypeptide
Results from interactions between amino acids and R groups
Four Levels of Protein Structure: Quaternary Structure
Overall protein structure
Made of two or more polypeptides
Proteins as a building material
a matrix of protein underlies almost all body structures → e.g. bones, muscles, ligaments, hair, nails, etc
New proteins are requires for growth and tissue maintenance → GI tract cells are replaced every 3 days, the whole body has its cells renewed every 7 years
Proteins as enzymes
Enzymes are usually composed of a protein, a vitamin, and a trace material
they act as catalysts, allowing reactions to occur more quickly and efficiently
An enzyme is not affected by the chemical reactions it allows the take place
Proteins as peptide hormones
Growth hormone
Insulin and glucagon
Thyroxin (amine hormone)
Calcitonin and PTH
ADH
(Fast-acting, short half-life)
Roles of Protein: regulation of fluid balance
Plasma proteins exert a colloid osmotic effect
pulling fluid from the tissue back into the blood
Roles of Proteins: acid-base regulation
Proteins act as buffers accepting and releasing hydrogen ions thus preventing acidosis or alkalosis
Transport proteins
Channels → e.g. Na+ and K+ channels
Carriers → e.g. glucose carrier
Active transporters → e.g. Na/K ATPase pump
Proteins in immunity
Antibodies are proteins that bind up specific invaders like viruses or antigens
antigens are substances that antibodies bind to. They may include bacteria, allergens, toxins, or anything that causes an inflammatory response
Roles of Proteins: source of energy
proteins can be broken down into amino acids and converted to other proteins
Some amino acids can be used within metabolism for energy
They can be also converted to sugars or stored as fats
Protein metabolism
Deamination is the removal of the nitrogen containing amino group, converting it to ammonia, which is sent to the liver and converted into urea. The remaining carbon fragment may be used for energy or stored as fat
amino acids can be used to make fat by removing the amino group and converting the remaining carbon fragments to fat
Other roles of protein
Can be converted to other proteins or make:
neurotransmitters norepinephrine and epinephrine
Melanin
Fibrin
Precursor to the vitamin niacin
Collagen (what it is and where’s its found)
Most abundant protein in vertebrates
Found in:
cartilage
Tendons
Bones
Teeth
Skin
Blood vessels
At least 18 different types of collagen
Collagen molecular structure
Molecules arranged in staggered pattern
Also relatively resistant to enzymatic breakdown
Types of Collagen (I, II, III, IV, V)
Type I → arteries, tendons, ligaments, skin, organs, bone
Type II → cartilage
Type III → alongside type I
Type IV → cell basement membranes
Type V → cell surfaces, hair, placenta
Vitamin C characteristics
Water-soluble:
cannot be stored for long (~ a month)
Symptoms can be seen 4-6 weeks after a deficiency begins (recovery is also relatively quick)
Most animals have the ability to make their own (not humans)
Elastin
Fibrous protein
Found in soft tissues → skin, blood vessels, and lungs
Elastin structure
Tropoelastin fibres → cross-linked
Random coil structure → little secondary structure
Very extensible
Elastic recovers
Proteoglycans
Hydrophilic molecules
Bonds with water
Allowing tissues to hold on to water → might otherwise be squeezed out by compression
Keratin
Hard, strong, but extensible
Made up of protein molecules → can align themselves into fibrous crystals
High stiffness (around 10GPa)
E.g. hair
Silk Protein - Fibroin
Form spider webs, cocoon, and nests
B-sheet structures
glycine on one hand
Alanine/serine on the other
Sheets stack on top of each other
Bulky regions interrupt sheets and allow for stretchiness
Hemoglobin characteristics
4 subunits containing Heme groups
contains iron for O2 binding
Each hemoglobin can bind 4 O2 molecules
Each RBC contains about 200 million molecules of hemoglobin
How hemoglobin is affected by pH
PH changes will affect affinity of Hb
High H+ (low pH) shifts curve to the right → decreases affinity for O2
allows for more unloading of O2 in the tissues
Bohr’s law
How hemoglobin is affects by CO2 and temp
High altitudes causes release of DPG (right shift)
Exercise:
higher temp, higher CO2, and higher H+ (lower pH)
These will shift curve to the right and decrease affinity of O2 for Hb
More unloading and O2 delivery to tissues
Fetal hemoglobin
Has a higher affinity for O2 than adult Hb
Can pull O2 from maternal RBC’s and move it to fetal RBC’s
Protein Energy
Daily normal requirement → 50g protein (10% of 2000kcal diet)
Proteins are needed for growth and maintenance and for fighting infections
acute protein energy malnutrition → children are thin for their height
Chronic protein energy malnutrition → children are short for their age