Chapter 3: Proteins Flashcards
What do protein chaperones do? why do they need to do this?
encourage proper protein folding; allows for different conformations/independent from cytosolic concentrations
What are the two secondary structures of proteins?
alpha helices + beta sheets
How often do H bonds occur between amino acids in an alpha helix?
every <4 amino acids
About how far apart are beta sheets?
~0.7 nm
What level of protein structure do domains typically occur as?
tertiary
What is a typical domain size in AAs?
40-350 AA
This is a specific portion of a protein that has known functions (whether that be catalytic, spacing, etc.)
domain
This is a specific subset of domians that are considered to be “genetically mobile”; can be found in many other proteins performing the same function
modules
What function does the Kringle module complete?
protein-protein interactions
What function does the immunoglobulin module complete?
antigen OR other protein/moleucle recognition
What function does the fibronectin type 3 module complete?
cell-to-cell interactions
What is the common function of an SH2 domain?
recognizes P-Tyrosine
Why are non-covalent bonds much more common between protein-protein/polypeptide-polypeptide interactions?
allow protein conformational changes without being “irreversible” like covalent bonding
What regions are the complementary structure of proteins sourced from?
R-regions of amino acids
The bonds between many actin modules to form actin fibers are usually ___? why?
weaker; allow for dynamic growth/shrinkage