ACEDS/ACTUAL EXAM LATEST VERSION WITH VERIFIED QUESTIONS AND ANSWERS GRADED A+
4 views 0 purchase
Course
ACEDS/ACTUAL
Institution
ACEDS/ACTUAL
ACEDS/ACTUAL EXAM LATEST
VERSION WITH VERIFIED
QUESTIONS AND ANSWERS GRADED A+
Henderson-Hasselbach Equation - ANS--pH = pKa + log ([A-] / [HA])
FMOC Chemical Synthesis - ANS--Used in synthesis of a growing amino acid
chain to a polystyrene bead. FMOC is used as a protecting group on the N-te...
FMOC Chemical Synthesis - ANS✔✔--Used in synthesis of a growing amino acid
chain to a polystyrene bead. FMOC is used as a protecting group on the N-terminus.
Collagen - ANS✔✔--Repeating sequence of Gly-X-Pro. 3 stranded "coiled coil".
Contains gly core.
Salting Out (Purification) - ANS✔✔--Changes soluble protein to solid precipitate.
Protein precipitates when the charges on the protein match the charges in the solution.
,Size-Exclusion Chromatography - ANS✔✔--Separates sample based on size with
smaller molecules eluting later.
Ion-Exchange Chromatography - ANS✔✔--Separates sample based on charge. CM
attracts +, DEAE attracts -. May have repulsion effect on like charges. Salt or acid used
to remove stuck proteins.
Hydrophobic/Reverse Phase Chromatography - ANS✔✔--Beads are coated with a
carbon chain. Hydrophobic proteins stick better. Elute with non-H-bonding solvent
(acetonitrile).
Affinity Chromatography - ANS✔✔--Attach a ligand that binds a protein to a bead.
Elute with harsh chemicals or similar ligand.
Low-Spin Fe - ANS✔✔--Electrons are less "spread out" and are compacted by
electron rich porphyrin ring.
T-State - ANS✔✔--Heme is in high-spin state. H2O is bound to heme.
R-State - ANS✔✔--Heme is in low-spin state. O2 is bound to heme.
SDS-PAGE - ANS✔✔--Uses SDS. Gel is made from cross-linked polyacrylamide.
Separates based off of mass with smaller molecules moving faster. Visualized with
Coomassie blue.
SDS - ANS✔✔--Sodium dodecyl sulfate. Unfolds proteins and gives them uniform
negative charge.
Isoelectric Focusing - ANS✔✔--Variation of gel electrophoresis where protein charge
matters. Involves electrodes and pH gradient. Protein stops at their pI when neutral.
FDNB (1-fluoro-2,3-dinitrobenzene) - ANS✔✔--FDNB reacts with the N-terminus of
the protein to produce a 2,4-dinitrophenol derivative that labels the first residue. Can
repeat hydrolysis to determine sequential amino acids.
Iodoacetate - ANS✔✔--Adds carboxymethyl group on free -SH groups. Blocks
disulfide bonding.
Homologs - ANS✔✔--Shares 25% identity with another gene
Orthologs - ANS✔✔--Similar genes in different organisms
, Paralogs - ANS✔✔--Similar "paired" genes in the same organism
.
α-helices - ANS✔✔--Ala is common, Gly & Pro are not very common. Side-chain
interactions every 3 or 4 residues. Turns once every 3.6 residues. Distance between
backbones is 5.4Å.
Helix Dipole - ANS✔✔--Formed from added dipole moments of all hydrogen bonds in
an α-helix. N-terminus is δ+ and C-terminus is δ-.
ß-sheet - ANS✔✔--Either parallel or anti-parallel. Often twisted to increase strength.
Parallel ß-sheet - ANS✔✔--Same sheet directions (C & N-termini line up). Has
angled H-bonds.
ß-turns - ANS✔✔--Tight u-turns with specific phi-psi angles. Must have gly at position
3. Proline may also be at ß-turn because it can have a cis-omega angle.
Loops - ANS✔✔--Not highly structured. Not necessary highly flexible, but can
occasionally move. Very variable in sequence.
Circular Dichroism - ANS✔✔--Uses UV light to measure 2° structure. Can be used to
measure destabilization.
Disulfide-bonds - ANS✔✔--Bonds between two -SH groups that form between 2° and
3° structure.
α-keratin - ANS✔✔--formed from 2 α-helices twisted around each other. "Coiled coil".
Cross-linked by disulfide bonds.
Hemoglobin 4° Structure - ANS✔✔--Tetramer. Dimer of dimers. α2ß2 tetramer.
α/ß Protein Folding - ANS✔✔--Less distinct areas of α and ß folding.
α+ß Protein Folding - ANS✔✔--Two distinct areas of α and ß folding.
Mechanism of Denaturants - ANS✔✔--Highly soluble, H-binding molecules. Stabilize
protein backbone in water. Allows denatured state to be stabilized.
The benefits of buying summaries with Stuvia:
Guaranteed quality through customer reviews
Stuvia customers have reviewed more than 700,000 summaries. This how you know that you are buying the best documents.
Quick and easy check-out
You can quickly pay through credit card or Stuvia-credit for the summaries. There is no membership needed.
Focus on what matters
Your fellow students write the study notes themselves, which is why the documents are always reliable and up-to-date. This ensures you quickly get to the core!
Frequently asked questions
What do I get when I buy this document?
You get a PDF, available immediately after your purchase. The purchased document is accessible anytime, anywhere and indefinitely through your profile.
Satisfaction guarantee: how does it work?
Our satisfaction guarantee ensures that you always find a study document that suits you well. You fill out a form, and our customer service team takes care of the rest.
Who am I buying these notes from?
Stuvia is a marketplace, so you are not buying this document from us, but from seller wambuip578. Stuvia facilitates payment to the seller.
Will I be stuck with a subscription?
No, you only buy these notes for $23.99. You're not tied to anything after your purchase.