BioChem TA Session Notes:

Monday 5-7 ch. 3-5.

Neutral pH 7.4 when they are dissaccociated and what is protonated and
what is unprotonoated and when.
Non polar amino acids sickle cell anemia polar glu to valline (nonpolar)
substitution.
Proline contains is a rigid ring containing a
Glycine along with succinly coA condenses in the formation fo the heme
moiety.
Glycine only amino that is not optically active
Uncharged amino acids: contribute to hydrogen bonding!!!!
Cysteine has a sulfer hydrl groups for disulfide bond
Many vessel proteins??? are stabilized by disulfide bonds (cysteine is needed)
Cytosol proteins do not need disulfide bonds.
Polar amino acids: tysosine is needed for the syntheses of many hormones.
Deanimated histidine becomes histidine.
Histidine is very important.
Albumin has a histinde (imizidol group) has a best buffering capacity.
Sugars are D
Amino acids is L
Amphoteric
pKa the pH at which that proton will actually leave.
Zwitter ion equal positive and negative charges. The pK is related to this.
Net zero: acidic are -1 and basic is +1 and memorise the acidic and basic
ones at neutral pH.
Henderson hasselback equation: concentration of the ionized and unionized
across a membrane.
Base becomes protonated it becomes iononzed then it cannot pass through
the membrane. (essentially you want the amino acids to become nonpolar so
that it can pass throught membrane)
Chapter 2
Formation of peptide bonds.
Break a peptide bond hydrolysis.
Peptide bond is rigdid and planar.
Partial double bond so there is not tortion/ rotation
Glucagon will raise your blood sugar.
Oxytosin milk ejection
More soluble when they are charged in zwitter ion form.
Conjugate proteins HDL/LDL and rodobsin.
What is the the biggest effector of how a protein will function/ and folded ?
Primary Structure!!!
Alpha amino end (N-terminal is the beginning) C terminal is the ending of the
amino acid chain.
HbM histidine is replaced my tyrosine
Cystic fibrosis mutation in the CFTR protein and the mutation is on the _____
position in the AA chain.
2Nd structure if formed by hydrogen bonding.
Full turn is 3.6 amino acids.

Proline disrupts the alpha helix and creates a bend. Also glysince but if both
ans present choose proline.
Globular proteins all beta sheets and right handed.
Antiparralel and parallel as based on the relative position of the N and the C
terminal.
Tertialry structure: stabilized by noncovalent interaction. Electrostatic and
ionic bonds.
Nonpolar amino acids cannot contribute to hydrogen bonding.
Quantanary structure:
Hemoglobin globual quandary protein.
Native confirmation is when they are completely folded. Protein is not
irreversible denatured the 2nd may break dwon or even the 3rd or 4th but the
primary structure will always remain.
Heat shock proteins
Disulfide isomerases.
Prions Disease: immporper fold ing of the protein. On surface of the gleal and
nerve cells.
The only things that makes these two problems so important is the folding of
the protein NOT the ACTUAL PRIMARY STRUCTURE