BIO 371 E2 LAB 13

Card Set Information

Author:
shockwave
ID:
149639
Filename:
BIO 371 E2 LAB 13
Updated:
2012-04-23 18:41:31
Tags:
BIO 371 E2 LAB 13
Folders:

Description:
BIO 371 E2 LAB 13 CELL GSU 2012
Show Answers:

Home > Flashcards > Print Preview

The flashcards below were created by user shockwave on FreezingBlue Flashcards. What would you like to do?


  1. PROTEINS SUCH AS ENZYMES ARE RENDERED UNFUNCTIONAL UPON UNFOLDING. WHY?
    FUNCTIONAL ACTIVITY IS DEPENDANT UPON THE PROTEINS NATIVE SHAPE.
  2. A NONCOLVALENT BOND TYPICALLY HAS ____ THE STRENGTH OF A COLVALENT BOND
    1/20
  3. THE SECONDARY STRUCTURES OF PROTEIN ARE STABLIZED BY WHAT?
    H+ BONDS BETWEEN THE O2 AND NH
  4. WHAT DO YOU FIND MORE SECONDARY TYPES OF B SHEET IN?
    PROTEINS THAT PREFORM NONSTRUCTURAL FUNCTIONS. ENZYMES AND Ab.
  5. ONE VERY IMPORTANT INTERACTION AT THE TERTIARY LEVEL IS WHAT?
    HYDROPHOBIC/HYDROPHILLIC SIDE CHAINS OF THE AMINO ACIDS RESIDUES.
  6. A MOLECULE OF HUMAN HEMOGLOBIN CONSISTS OF WHAT?
    4 POLYPEPTIDE CHAINS HELD TOGTHER VIA NONCOLVALENT BONDS. A QUATERNARY STRUCTURE.
  7. INTRA-CHAIN DISULFIDE BONDS STABILIZE _____.
    INTER-CHAIN DISULFIDE BONDS STABILIZE _____.
    • INTRA: TERTIARY
    • INTER: QUADERNARY
  8. IN AN ACID SOLUTION WHAT IS THE CHARGE ON THE AMINO GROUPS? CARBOXYLS?
    • POSITIVE.
    • NOTHING. NOT IONIZED.
  9. 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.
  10. MOST NEUTRAL AMINO ACIDS HAVE A pI AROUND WHAT?
    6.0
  11. 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.
  12. 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.
  13. AT A POINT ABOVE IT'S pI, A PROTEIN BECOMES WHAT?
    NEG CHARGED.
  14. 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.
  15. WHAT THE HELL DOES THE ANIONIC DETERGENT SDS STAND FOR?
    SODIUM DODECYL SULFATE
  16. 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
  17. WHEN A PROTEIN LOSES IT'S NEGATIVE CHANGE, IT'S CALLED WHAT?
    DENATURED.
  18. 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.
  19. 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.
  20. 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
  21. 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.
  22. NAME A REDUCING AGENT
    B-MERCAPTOETHANOL
  23. THE MOST COMMONLY USED STAIN FOR THE DETECTION OF PROTEINS IS WHAT?
    WHAT DOES IT CONTAIN?
    • COOMASSIE BLUE
    • ACETIC ACID
  24. PEPTIDE GENERATED BY PROTEINS EXPOSED TO CHYMOTRYPSIN START WITH WHAT 3 AA?
    • VALINE..VAL
    • GLUTAMIC ACID....GLU
    • GLUTAMINE...GLN

What would you like to do?

Home > Flashcards > Print Preview