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
what is the main function of proteins
defense, movement, signaling, structure, transport, and act as catalysts (enzymes)
how do you categorize amino acids based on their R Groups
- charged
a. acidic= negative charge
b. basic=positive charge - uncharged polar- have oxygen and are uncharged
- nonpolar- no oxygen present and no charges
