CH 3 Flashcards
(17 cards)
How do amino acids react to water
In pH 7 water, amino acids IONIZE
- it causes the amino group to act as a base & attracts a proton to form NH3+
- the carboxyl group then acts as an acid
why are the charges on the function groups of amino acids important
(1) They help amino acids stay in solution, where they can interact with one another and with other solutes,
(2) they affect the amino acid’s chemical reactivity.
Function of amino acids with side chains that have no functional groups
- they consist solely of carbon & hydrogen atoms
- rarely participate in chemical reactions
- influence primarily depends on size & shape rather than reactivity
Hydrophilic R-groups
polar & electrically charged
Hydrophobic R-groups
nonpolar lacking charge & highly electronegative atoms capable of forming hydrogen bonds with water
acidic r-groups
- has a negative charge & lost a proton
- e.g. aspartate
basic r-groups
- positive charge & picked up a proton
- e.g. lysine
uncharged polar r-group
- has highly electronegative oxygen that will form a polar covalent bond in the r group
- e.g. serine
Why are peptide bonds unusually stable
the nitrogen can intermittently donate its pair of unshared valence electrons to the carbon in the C-N bond
How do R-groups affect each amino acid
size, shape, chemical reactivity, & solubility
- properties & function
secondary structures
- H bonding occurs btwn oxygen on carbonyl (- charge) of one amino acid residue & the H (+ charge) on the amino group of another
dimer
proteins with 2 polypeptide subunits
macromolecular machines
a group of proteins, & possibly other nonprotein macromolecules, that assemble to carry out a particular function
does protein folding tend to be spontaneous
yes
- this occurs when a chain is placed in an aqueous solution
hydrophobic interactions with proteins
drive proteins to fold such that their nonpolar R-groups coalesce (join) in the interior
- increases entropy of the surrounding water
- folded molecule has less potential energy = more stable
molecular chaperones
a protein that facilitates the folding or refolding of a protein into its correct 3D shape
- heat-shock proteins
- attach to hydrophobic patches before aggregates can form
prions
- proteinaceous infectious particles
- infectious particle that consists entirely of protein
- adopt a normally folded shape & an infectious, often disease-causing shape
- can bind normally folded prion proteins & cause them to adopt infectious shape