What is the only aa that has buffering properties
Histidine, sits at ph 6-7
Tryptophan is a precursor to what molecule
Serotonin
What molecule is a major player in tryptophan being able to cross the blood brain barrier
Insulin, generally from response to high carb diet
What is the primary excitatory neurotransmitter of the CNS
Glutamate
What functions is glutamate a key player in
Pain sensation
Neuronal plasticity
Central sensitization
What does the primary structure of a protein determine
Shape AND function
What is the importance of substance p
It is a neuropeptide that is co- released with glutamate to create a greater sense of pain and injury in the system.
What number of aa corresponds with a polypeptide
10-20 aa
What number of aa corresponds to proteins
> 20 aa
What are the functional classes of proteins
Enzymes Transport Mechanical support Contractile Control and signaling
What is the cause of sicke cell anemia
A non conservative change of a Hb protein of glutamate, for valine
What aa h-bond together in an alpha helix
1st and 5th
What is average distance between turns when h-bonding occurs in an alpha helix
3.6aa/ turn
Why is the anti parallel nature of beta sheets stronger than a parallel structure
The h bonds are closer together in a anti parallel structure, while there is a slightly larger distance between the bonds in a parallel structure, thus making the bonds weaker
Where is beta sheeting often found
Inside the cell, and often pulls proteins together
Which secondary structure makes up half of the globular proteins
Beta sheeting
What is the predominant aa in the collagen triple helix
Glycine- approx every 3rd aa in the chain
What is the basic unit of collagen
Tropocollagen
What is the basic structure of tropocollagen
3 separate peptide chains held together by interchain h bonds
A polyproline strand will form what structure
A TRIPLE helix
What factor is required for proper collagen formation
Vitamin c, lack of will lead to scurvy
What causes cross linking in collagen
Losing residues
Larger amounts cause aging
Lack of cross linking causes stretchy skin
What is the specific structure of protein due to
Hydrophobic bonding
Specific side chain interactions
What is the strongest 3* structure interactions
Disulfide bridges
What is the weakest 3* interaction
Van der waals forces
How does urea denature a protein
Out-competes for h bonding of protein structures at all levels
How many bonds are needed for a biuret reaction to occur
At least 2 peptide bonds
What does hydrolysis and proteases do to protein
Denatures by breaking peptide bonds
How can you separate out individual proteins
Gel electrophoresis
What molecule musts specifically be present for o2 to bind a Hb
Fe2+
Must be present in the heme group of Hb
Why doesn’t met Hb bind O2
Because it contains Fe3+
What is the better O2 carrier in the body
Mb because it only has one heme group to bond it’s able to deliver O2 faster ( creates a left shifted curve)
How does CO2 affect the function of Hb
Lowers the affinity for O2 but does not directly bind the heme group. ( binds the nh3 end)
How does CO affect O2 transport
Directly competes for the heme group and binds to fe2+
Able to displace o2 at low concentrations
What is the Bohr effect
Higher h+ levels causes decree in o2 affinity for the heme group allowing more o2 to be released into the body.
Important when metabolically active and body creates slight acidic environment
What is the affect of BPG
Binds two subunits of Hb causing lowered affinity of o2 and a right shift on the graph
What are the affects of fetal Hb
Does not bind BPG, so you get a left shifted graph
What is HbA1c used for
Long term view of blood glucose levels
What are the types of chains making up the shape of the antibodies
2 heavy chains
2 light chains
What is the predominant structure of the antibody
Beta sheeting domains
How is the antibody held together
Disulfide bridges
Where are the binding sites for antigens located on the antibody
On the variable region at two identical sites
