Protein Folding Flashcards
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
two types of secondary structure
alpha helix
beta pleated sheet
Alpha helix
more flexible secondary structure
coiled backbone
used in fingernails and toenails
Beta pleated sheet
more rigid
able to stack on top of themselves
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
What does protein denaturation show?
Shape is important
if shape is altered, function becomes altered
How can proteins be denatured?
temperature and pH change
When can proteins no longer be returned to normal?
when disulfide (strong bonds) are broken
Common example of protein denaturation
cooking eggs
Chaperones
other proteins that facilitate proper folding
Prions
misfolded rogue proteins that alter the folding of other proteins
example of prion
mad cow disease
Quaternary structure
the organization of 2 or more polypeptide subunits in 3D space
Sickle cell anemia
the shape of proteins
Where can hydrogen bonds be formed to create secondary structure?
Between every 4th amino acid
