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Bio Chem 3100 Exam One Questions And 100% Correct Answers
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Bio Chem 3100 Exam One Questions And 100%Correct Answers
Reproduction
Ability to produce new organisms.
Organization
Proteins, carbohydrates, lipids, nucleic acids, water, vitamins and minerals
Metabolism
Synthesis and breakdown of macromolecules with the release and utilization of energy
Anabolism vs Catabolism
Anabolism: Synthetic pathways; extract energy from environment
Catabolism: Degradation pathways; release energy by breakdown of carbohydrates to
maintain internal environment and perform vital functions
Growth
Increase in size in all of its part rather than just accumulating matter
Respond to stimuli
Able to sense and respond to alterations in the surroundings.
Homeostasis
Regulation of internal environment to maintain a constant state
,Adaption
The ability to change over a period of time in response to environment. Undergo
evolution.
What constituents does the mobile phase have in chromatography?
The mobile phase can be either organic/inorganic solvent or buffer solution with
different variables.
What is column chromatography used for?
Column chromatography separates a mixture of proteins based on a porous solid phase
and a liquid phase that moves the proteins.
How does the column chromatography separate proteins of differing affinities?
Those proteins that have a lower affinity for the solid phase wash off earlier, while those
that have a higher affinity remain on the column longer and wash off later.
What else is size-exclusion chromatography known as?
'gel filtration' or 'molecular sieving.'
On what basis does size-exclusion chromatography separate protein molecules?
It separates protein molecules based on their molecular weight or 'Stokes radius.'
What are the beads of size-exclusion chromatography made of?
These beads consist of polymers of acrylamide or dextran or agarose and are of uniform
pore size.
What happens to large protein molecules in the course of size-exclusion
chromatography?
The large protein molecules are too big to enter the pores of the beads and so travel
between the beads, eluting first, being 'excluded' from inside the beads.
,What happens to small protein molecules in the course of size-exclusion
chromatography?
Small protein molecules enter the pores of the beads and travel slowly through the
interbead space, being 'included' in the beads. They elute later according to their size,
the smaller molecules eluting last.
Ion-exchange chromatography separates protein molecules based upon their overall
net charge. Question Anionic proteins Anionic proteins have more negatively charged
residues than positively charged residues and have a pI < 7.0. Cationic proteins?
Cationic proteins have more positively charged residues than negatively charged
residues and, therefore, possess a pI greater than 7.0.
What are ion-exchange resins, and what is attached to their surface?
Ion-exchange resins have charged groups attached covalently on their surface.
What are cation exchangers, and can you give examples?
Cation exchangers have negatively charged groups attached on their surface. Ex:
CM-cellulose, Phosphocellulose, and SP-Sepharose.
What are anion exchangers, and can you give examples?
Anion exchangers have positively charged groups attached to its surface. Ex:
DEAE-Sephadex, TEAE-Sepharose, and Q-Sepharose.
What type of proteins bind tightly to the cationic and anionic exchangers?
Cationic proteins bind tightly to cationic exchangers.
Anionic proteins bind tightly to anionic exchangers.
At what pH and ionic strength the binding of proteins to the ion-exchange resin is
performed?
Neutral pH and low ionic strength.
, How the non-specifically bound proteins washed off in ion-exchange chromatography?
At low ionic strength.
How do bound proteins elute from the ion-exchange column?
By increasing the ionic strength.
What is the basis for separating protein molecules in size-exclusion, ion exchange and
hydrophobic interaction chromatographies?
Small differences in their physico-chemical properties.
What is necessary to purify a certain protein fast and efficiently?
It has to use a unique property of the protein.
How does affinity chromatography purifies proteins?
It uses the biological function for the purification of a protein.
What is another term for affinity chromatography?
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