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Flashcards in Ch. 3 Review Deck (16)
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1

What is dialysis?

Diluting small molecules out of a dialysis bag and leaving protein molecules.

2

What is gel-filtration?

-it is based on size of molecule
- basically a diffusion of small and large molecules through carb polymers to separate protein molecules

*large molecules make it to bottom 1st because they are large and pass by the polymers
**small molecules are small enough and have to go through the polymers loops so it takes longer henceforth they are last

3

What is ion-exchange?

-anion + cation exchanges

-positively charge AA bind to negative charged beads while negative charged AA flow through

4

What is affinity?

Addition of glucose to separate glucose binding AA from glucose residues on beads

5

What is isoelectric focusing?

An electrophoretic technique for the separation of proteins based on their isoelectric point (pI).

The pI is the pH at which a protein has NO NET CHARGE and thus, does not migrate further in an electric field.

6

What does SDS-PAGE stand for?

Sodium dodecyl sulfate - polyacrylamide gel electrophoresis

7

What does ELISA stand for?

Enzyme-linked immunosorbent assay

8

Difference between ELISA and western blotting?

ELISA is more rapid + requires less steps

9

What do ELISA and western blotting have in common?

Both are used to detect antibodies

*HIV testing

10

Methods of protein sequencing

Edman degradation

Mass spec-ESI OR MALDI-TOF

11

How does cyanogen bromide work?

Cleaves the carboxyl side of methionine residues

12

How does trypsin work?

Cleaves carboxyl sides of lysine and arginine residues

13

How does Chymotrypsin work?

Cleaves carboxyl side of tyrosine, tryptophan, phenylalanine, leucine, and methionine

14

How does carboxypeptidase A work?

Cleaves carboxyl side of all amino acids EXCEPT arginine, lysine, or proline.

15

Function of DTT and BME?

Breaks di-sulfide bonds

16

How can we determine a 3D structure of a protein?

X-Ray crystallography and NMR