proteins part 2 Flashcards
the combo of multiple peptides together, or the combo of peptides with non protein molecules
quaternary structure
multiple peptide subunits joined together
polypeptide
single peptide alone
monomer
two peptides joined together
dimer
the stability of a protein depends on
its environment, its intermolecular forces, and it intramolecular forces
proteins fold into a state that BLANK the entropy of the system and BLANK their own intrinsic energy
maximizes, minimizes
a low energy protein is a BLANK protein
more stable
in an aqeuous environment, hydrophilic residues will want to be positioned on the BLANK of a protein
outside
at a high ph, more of the proteins residues will be
deprotonated
changing the BLANK away from their optimal values will result in unfolding of a native state protein into a denatured and functionally inactive form
temperature, salinity, or pH
on the interior of the protein, what kind of R groups are able to interact favorably to maximize the stability of the protein
hydrophobic
the extent to which a system is disordered, spread out, and chaotic
entropy
the universe want more or less entropy
more
