Proteins

Question 1

This maintains the cellular shape and integrity

Answer 1

Cytoskeleton

Question 2

Proteins are born in translation and matures thru __________ modification

Answer 2

Posttranslational

Question 3

___________ factors alternate between working and rest state.

Answer 3

Regulatory

Question 4

Proteins ages thru what process?

Answer 4

Oxidation and deamination

Question 5

What is the protein needed for determination of physical and functional protein properties?

Answer 5

Highly purified protein

Question 6

Isolation of proteins using differences in relative solubility of individual proteins as a function of pH

Answer 6

Isoelectric precipitation

Question 7

Isolation of proteins using differences in relative solubility of individual proteins as a function of polarity

Answer 7

Precipitation with ethanol and acetone

Question 8

Isolation of proteins using differences in relative solubility of individual proteins as a function of salt conc

Answer 8

Salting out with ammonium sulfate

Question 9

What are the two phases that partition molecules in chromatography?

Answer 9

Mobile and stationary phase

Question 10

Protein interacting more strongly with the ________ phase are retained longer

Answer 10

Stationary

Question 11

A protein mixture is applied to column and liquid mobile phase is percolated thru it, small portion of eluant/mobile phase are collected

Answer 11

Column chromatography

Question 12

In column chromatography, the matrix interact withproteins based on 3 properties which are?

Answer 12

1. Charge
2. Hydrophobicity
3. Ligand-binding properties

Question 13

Separation of mixtures in columns based on partition of a solute between 2 solvents

Answer 13

Partition chromatorgraphy

Question 14

Separates proteins based on their stoke radius or sphere diameter

Answer 14

Size exclusion chrom

Question 15

Size exclusion chromatography is also known as

Answer 15

Gel filtration

Question 16

In SEC, protein emerged via ___________ order of their stokes radii( func of molecular mass and shape)

Answer 16

Descending

Question 17

Proteins are sequentially released by disrupting the forces that stabilize the protein stationary phaseusing a gradient of increasing salt conc

Answer 17

Absorption chrom

Question 18

Proteins interact with the stationary phase via charge-charge interactions

Answer 18

Ion exchange chrom

Question 19

Proteins with exposed hydrophobic surfaces adhere to the matrix via hydrophobic interactions enhanced by a mobile phase of high ionic strength

Answer 19

Hydrophobic interaction chrom

Question 20

This type of chrom exploits the high selectivity of most proteins for their ligands

Answer 20

Affinity chrom

Question 21

Most powerful and widely applicable affinity matrices are used for?

Answer 21

Recombinant protein purification

Question 22

Chrom that employs incompressible silica and alumina microbeads as stationary phase and pressures up to thousand psi, permitting high flow rates and enhanced resolution

Answer 22

High pressure liquid chrom

Question 23

I most widely used method for determing protein purity that uses dodecyl sulfate

Answer 23

Polyacrylamide gel

Question 24

In Isoelectric focusing, ionic buffers called _______ and an applied electric field are used to generate pH gradient within a polyacrylamide matrix

Answer 24

Ampholytes

Question 25

Separated insulin chains by reducing the disulfide bonds and cleaved with trypsin, chymotrypsin and pepsin

Answer 25

Sanger amino acid sequencing

Question 26

Fredirick Sanger won the Nobel prize for determining the aa sequence of________

Answer 26

Insulin

Question 27

Pehr Edman introduced __________ or Edman’s reagent

Answer 27

Phenylisothiocyanate

Question 28

Succesive rounds of derivatization wih Edman’s reagent can be used to sequence the first ________ residues

Answer 28

20-30

Question 29

Posttranslational modification of proteins identified via mass increments.

Answer 29

Mass spectrometry

Question 30

Discriminates molecules based only on mass

Answer 30

Mass spectrometry

Question 31

It is the spatial relationship of every atom in a molecule

Answer 31

Conformation

Question 32

This is the geometric relationship between atoms ( L-aa and D-aa)

Answer 32

Configuration

Question 33

Structure of protein made up of aa sequences that provides both molecular fingerprint for ID and information.

Answer 33

Primary structure

Question 34

What composed the amino acid structure?

Answer 34

A-Carbon atom, amino grp, carboxyl grp, R side chain, H ion

Question 35

Proteins contain exclusively what optical isomer?

Answer 35

L-amino acids

Question 36

What are the polar -OH grp amino acids?

Answer 36

Serine, threonine, tyrosine

Question 37

Amino acids containing amino group

Answer 37

Asparagine and glutamine

Question 38

Amino acids that contains sulfur

Answer 38

Methionine and cysteine

Question 39

Amino acids that contain aromatic rings?

Answer 39

Phenylalanine, tryptophan, tyrosine,histidine

Question 40

It is an imino acid

Answer 40

Proline

Question 41

Smallest amino acid found in peptide bends

Answer 41

Glycine

Question 42

These are amide linkages that binds amino acids together

Answer 42

Amide linkage

Question 43

Give examples of proteins

Answer 43

Cytoskeleton, actin/myosin, hemoglobin, immunoglobulins, enzymes, receptors