Chapter 1
Chapter 2
Chapter 3
Chapter 4
Vocabulary
100
DNA -gene expression--->transcription --mRNA--> translation in ribosome ------> protein folding (function depends on shape // gene sequence is important)
What is the Central Dogma?
100
a molecule having a partial negative charge on oxygen with two lone pairs covalently attached to two hydrogens adopting partial positive charges.
What is a water molecule?
100
can form from other molecules called ampholytes, or amphoteric compounds and can act as both an acid and a base.
What is a Zwitterionic form?
100
A peptide bond may
not freely rotate
100
nonprotein compound // used to designate an organic cofactor // necessary for the function of that enzyme
coenzyme
200
enchance biological rxns, decrease activation energy, NEVER change equalibrium, and don't get used up
What can enzymes do for a biochemical reaction?
200
good solvents for water
What are polar/charged molecules?
200
The polypeptide chain bond can freely rotate.
not at the polypeptide bond. phi and psi bonds rotate
200
Primary, secondary, tertiary, and quaternary
What are the 4 protein level structure?
200
the structural unit of an oligomeric protein (subunits are identical)
protomer
300
delta G = delta H - Temperature in Kelvin delta S is free energy change.
Endergonic
Exergonic
Endothermic
Exothermic
unfavorable
favorable
absorb heat - reaction is cooler than the surrounding
release heat - reaction is hotter than surrounding
300
hydrogen bonds
ionic interactions
hydrophobic/philic interactions
Van der Waals
What are 4 weak interactions?
300
proteins coming down a column to purify it based on size using beads.
The large proteins would flow fast down and would not be kept in the column.
what is size-exclusion chromatography?
300
heat and cold
pH extremes
organic solvents
chaotropic agents: urea and guanidium hydrochloride
What can denature proteins?
300
nonprotein group // covalently attached cofactors
prosthetic group
400
-30.5 jK/mol of free energy that allows a reaction to become more favorable
What is ATP?
400
Isotonic
Hypertonic
Hypotonic
What are the 3 cases that may happen based on the osmolarity?
400
Using TCEP can break what bonds?
What are disulfide bonds?
btw, what are the two amino acids with S in their R groups?
400
An experiment using a small protein that contains 8 cystines linked via four disulfide bonds. In the presence of 2-mercaptoethanol and urea the disulfide bonds break and in absence of these chemicals they reform
What is the experiment of ribonuclease refolding experiment?
400
a functional non amino acid component such as
metal ions or organic molecules
cofactor
500
What is ATP?
500
It equals 14 when added together.
What is pH and pOH?
500
Successive rounds of Nterminal
What is Edman degradation?
500
London forces
Electrostatic
Hydrogen bonds
Hydrophobic effect
What are 4 weak interactions in proteins?
500
not all proteins fold spontaneiously therefore these facillitate correct folding pathways // provided mirco enivrionment for folding
chaperones