Chapter 3 terms Flashcards
polymerize
process of many monomers coming together to form a polymer
peptide bond
what hold together amino acids and primary structure
oligopeptide
fewer than 50 amino acids
what are the three types of R groups
- charged (hydrophobic)
- uncharged polar (hydrophilic) have oxygen and uncharged
- nonpolar (hydrophobic)no oxygen present and no charges
primary structure
sequence of amino acids held together by peptide bonds
secondary structure
folding starts to occur; alpha helix and beta pleated sheets; hydrogen bonds
tertiary structure
3D folding; hydrophilic on outside of fold and hydrophobic on inside of fold; held together by bonds and interactions of R groups and peptide backbone
quaternary structure
protein with more than 1 polypeptide chain; held together by bonds and interactions between r groups and peptide backbones of different polypeptides
denaturation
process of unfolding and breaking down of protein; protein loses shape due to too high or low of temp or change in pH (normal conditions changed)
disulfide bonds
bridge between sulfhydryl groups
molecular machines
multiple proteins; carry out particular function/task; 1 specific function
dimer
2 protein monomers
prions
improperly folded forms of normal proteins; shape different, but amino acid sequence does not differ
trimer
3 protein monomers
molecular chaperones
helps proteins fold correctly in cells
