what are the different types of globular proteins?
What are the different kinds of structural proteins?
types of covalent bonds?
peptide and disulfide
types of non-covalent bonds?
hydrophobic interactions
hydrogen bonds
ionic bonds
What amino acids will participate in hydrophobic interactions?
valine, leucine, isoleucine, alanine
and phenylalanine
What do hydrogen bonds do during protein folding?
stabilize the secondary structures of a-helix and b-sheet
Hydrogen bonds between amino acid side chains
stabilize the tertiary structure of proteins
What is the purpose of chaperones or heat shock protiens?
What is the function of Hsp 70?
prevents the aggregation of unfolded protein.
It binds to hydrophobic regions of an extended
polypeptide and prevents premature folding of
a protein
What is the function of Hsp 60?
have a barrel shape and are required for correct folding of cellular proteins that do not fold spontaneously
Hsp 60 can be used to aid refolding of a protein after it has crossed a cellular membrane.
This needs ATP
Ubiquitin-Proteasome Complex
Misfolded or defective proteins are normally tagged
by the small protein ubiquitin and degraded in the
ubiquitin-proteasome system
ATP dependent
When does piron disease occur?
When the normal prp protein changes 3-D conformation due to changes in secondary structure
normal prp = more alpha helices
mutated prp = more beta sheets
Routes of transmission of piron disease?
How can hydrogen bonds be broken?
high temperature, 5-10 M urea, or salt
how are hydrogen and ionic bonds broken?
strong acids or bases.
How are hydrophobic interactions broken?
1-2% of the detergent Sodium dodecyl sulfate (SDS)
How are disulfide bonds broken?
β-mercaptoethanol