Bonds between amino acids flat

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Reference no: EM133261159

1. Why are bonds between amino acids "flat"?

ALL OF THESE

NONE OF THESE

Because of their partial double-bond character

All carbon-nitrogen bonds are planar.

Long-distance bonding between the nitrogen and oxygen limits movement.

2. Gradient centrifugation is commonly used for which of the following?

isolating small molecules

measuring the concentration of proteins in a solution

separating organelles out of a homogenate

separating proteins in a solution

3. 2-D electrophoresis involves

affinity chromatography and SDS-PAGE

isoelectric focusing and affinity chromatography

isoelectric focusing and ion-exchange chromatography

ion-exchange chromatography and SDS-PAGE

isoelectric focusing and SDS-PAGE

4. Some amino acids are called "nonessential" because

your body can make them

they are not necessary for your health

you can eat them

you have so many of them

they are not used to make proteins

5. Alpha helices, beta sheets, and turns are examples of......structure.

secondary

tertiary

primary

quaternary

6. Which of the following would have the most entropy?

molten globule

unfolded polypeptide

amyloid fibril

beta sheet

alpha helix

7. Which of the following can change the proteins found in a cell?

environmental conditions

NONE OF THESE

ALL OF THESE

enzymatic modifications

developmental stage

8. Which of the following can serve as antigens?

proteins and polysaccharides

proteins and small molecules

polysaccharides and ions

ALL OF THESE

ions and small molecules

NONE OF THESE

9. Essential amino acids are....

hydrophilic

the 20 that proteins are made of

polar

hydrophobic

important parts of your diet

10. Which of the following is NOT true of immunoprecipitation?

A) separates particles using an electric field

B) uses antibody-coated beads

C) good for isolating specific proteins from a solution

D) includes a denaturing step

11. Protein size is often determined using...

A) isoelectric-focusing gel

B) Edman degradation

C) SDS polyacrylamide gel electrophoresis

D) affinity chromatography

E) ELISA

12. Which of the following states of a protein would be the most stable?

A) amyloid fibril state

B) molten globule state

C) unfolded state

D) intermediate state

E) native state

13. Which pair of amino acids are negatively charged at pH 7?

A) glutamine and histidine

B) aspartic acid and glutamate

C) lysine and arginine

D) alanine and glutamate

E) lysine and proline

14-Which of the following qualities is most frequently used to measure the amount of a substance in a solution?

A) shape

B) density

C) size

D) weight

D) light absorbance

15. According to convention, the terminus is drawn on the left side of a peptide.

5'

carboxy

amino

3'

16. Which of the following is the usual order in the process of protein purification?

centrifugation, homogenation, chromatography, electrophoresis

homogenation, chromatography, electrophoresis, centrifugation

homogenation, electrophoresis, centrifugation, chromatography

homogenation, centrifugation, chromatography, electrophoresis

17. Which of the following is characterized by "multiple subunits"?

secondary structure

tertiary structure

quaternary structure

protein

primary structure

18. Misfolded proteins are not responsible for....

Alzheimer Disease

Parkinson Disease

Huntington Disease

kwashiorkor

prion disease

19. The protein structure where a series of amino acids are each bonded with the fourth amino acid down the chain is the....

alpha helix

beta sheet

coiled coil

turn

20. Which of the following amino acids would be LEAST likely to be found on the surface of a globular protein?

lysine

glutamine

serine isoleucine

cysteine

Reference no: EM133261159

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