-
PROTEINS SUCH AS ENZYMES ARE RENDERED UNFUNCTIONAL UPON UNFOLDING. WHY?
FUNCTIONAL ACTIVITY IS DEPENDANT UPON THE PROTEINS NATIVE SHAPE.
-
A NONCOLVALENT BOND TYPICALLY HAS ____ THE STRENGTH OF A COLVALENT BOND
1/20
-
THE SECONDARY STRUCTURES OF PROTEIN ARE STABLIZED BY WHAT?
H+ BONDS BETWEEN THE O2 AND NH
-
WHAT DO YOU FIND MORE SECONDARY TYPES OF B SHEET IN?
PROTEINS THAT PREFORM NONSTRUCTURAL FUNCTIONS. ENZYMES AND Ab.
-
ONE VERY IMPORTANT INTERACTION AT THE TERTIARY LEVEL IS WHAT?
HYDROPHOBIC/HYDROPHILLIC SIDE CHAINS OF THE AMINO ACIDS RESIDUES.
-
A MOLECULE OF HUMAN HEMOGLOBIN CONSISTS OF WHAT?
4 POLYPEPTIDE CHAINS HELD TOGTHER VIA NONCOLVALENT BONDS. A QUATERNARY STRUCTURE.
-
INTRA-CHAIN DISULFIDE BONDS STABILIZE _____.
INTER-CHAIN DISULFIDE BONDS STABILIZE _____.
- INTRA: TERTIARY
- INTER: QUADERNARY
-
IN AN ACID SOLUTION WHAT IS THE CHARGE ON THE AMINO GROUPS? CARBOXYLS?
- POSITIVE.
- NOTHING. NOT IONIZED.
-
IN STRONG ALKALINE SOULTIONS, WHAT CHARGE DOES THE AMINO GROUPS HAVE?
IN BASIC SOLUTIONS THE AMINO GROUPS HAVE NEGATIVE CHARGES AND THUS MIGRATE TO THE POSITIVE TERMINALS OF THE GEL RUN.
-
MOST NEUTRAL AMINO ACIDS HAVE A pI AROUND WHAT?
6.0
-
pI OF ACIDIC AA ARE CLOSE TO WHAT? WHAT DOES THIS MEAN WHEN THEY ARE IN pH OF 6?
- ACIDIC AA pH=3.
- WHEN IN pH6, THEY CARRY A NNEG CHARGE, AND GOTO POS TERMS.
-
pI OF BASIC AA ARE CLOSE TO WHAT? WHAT DOES THIS MEAN WHEN THEY ARE IN pH OF 6?
- 10
- AT pH6, THEY HAVE A POSITIVE CHARGE AND GOTO NEG TERMINAL IN GEL.
-
AT A POINT ABOVE IT'S pI, A PROTEIN BECOMES WHAT?
NEG CHARGED.
-
THE RATE OF MIGRATION OF A PROTEIN SPECIES THRU AN ELECTRICAL FIELD DEPENDS ON WHAT?
- CHARGE DENSITY.
- HIGHER = FASTER RATE.
- EX: IN pH OF 8.6
- ALBUMIN pI = 4.7 VS GLOBIN pI=7.2.
- ALBUMIN HAS MORE NEG CHARGE, FROM pH OF 8.6, THUS FATER.
-
WHAT THE HELL DOES THE ANIONIC DETERGENT SDS STAND FOR?
SODIUM DODECYL SULFATE
-
T OR F ?
SDS DOES NOT WORK ON THE DISULFIDE BONDS OF A PROTEIN AND MUST BE INTRODUCED TO A REDUCING AGENT IN ORDER TO BECOME CLEAVED.
TRUE
-
WHEN A PROTEIN LOSES IT'S NEGATIVE CHANGE, IT'S CALLED WHAT?
DENATURED.
-
ELECTROPHORETIC SEPERATION OF ______ PROTEINS SORTS THEM OUT BY SIZE.
WHY NOT CHARGE?
- DENATURED
- BECAUSE IT RELIES ON THE ABILITY OF UNIFORM CHARGE. THE SDS AND THE B-MERCAPTOETHANOL REDUCE CHARGES.
-
WHAT THE HELL IS AGAROSE GEL MADE OF?
POLYSACCHARIDE OF GALACTOSE AND 3,6-ANHYDROGALACTOSE DERIVED FROM AGAR, WHICH IN TURN IS OBTAINED FROM CERTAIN MARINE RED ALGAE.
-
THE MIGRATION OF A PROTEIN THRU AGAROSE GEL IS DEPENDANT MAILY ON WHAT?
NAME 3!
- THE NET ELECTRICAL CHARGE ON THE PROTEIN.
- THE INTENSITY OF THE ELECTRICAL FIELD.
- pH & IONIC STRENGTH OF THE BUFFER
-
THE SEPERATION OF PROTEINS BASED ON MOLECULAR WEIGHT IS HIGHLY DEPENDANT UPON WHAT?
NAME 2 POINTS.
- THE DENATURATION WITH SDS
- THE pH OF THE BUFFER.
-
NAME A REDUCING AGENT
B-MERCAPTOETHANOL
-
THE MOST COMMONLY USED STAIN FOR THE DETECTION OF PROTEINS IS WHAT?
WHAT DOES IT CONTAIN?
- COOMASSIE BLUE
- ACETIC ACID
-
PEPTIDE GENERATED BY PROTEINS EXPOSED TO CHYMOTRYPSIN START WITH WHAT 3 AA?
- VALINE..VAL
- GLUTAMIC ACID....GLU
- GLUTAMINE...GLN
|
|
