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Flashcards in Protein Folding Deck (16):
1

What forces stabilize protein folding?

hydrogen bonds can form between nearby amino and carboxyl groups on the SAME polypeptide chain

this can happen within the backbone itself

2

two types of secondary structure

alpha helix

beta pleated sheet

3

Alpha helix

more flexible secondary structure

coiled backbone

used in fingernails and toenails

4

Beta pleated sheet

more rigid

able to stack on top of themselves

5

Tertiary structure

the 3D shape of a protein created through R-group interactions

ex: if the r-groups are nonpolar, van der waals interactions will take place

6

What does protein denaturation show?

Shape is important

if shape is altered, function becomes altered

7

How can proteins be denatured?

temperature and pH change

8

When can proteins no longer be returned to normal?

when disulfide (strong bonds) are broken

9

Common example of protein denaturation

cooking eggs

10

Chaperones

other proteins that facilitate proper folding

11

Prions

misfolded rogue proteins that alter the folding of other proteins

12

example of prion

mad cow disease

13

Quaternary structure

the organization of 2 or more polypeptide subunits in 3D space

14

Sickle cell anemia

the shape of proteins

15

Where can hydrogen bonds be formed to create secondary structure?

Between every 4th amino acid

16

Sickle cell anemia

caused by a single point mutation that changes the primary amino acid sequence

this results in sickle celled hemoglobins

can block blood flow