drexel bio 209 final exam
weak interactions - ANS-electrostatic
h bonding
van der waals
hydrophobic effect- tendency of non polar molecules to avoid contact with water in aqueous
solutions
chemical bonds - ANS-strong- covalent ( enzymes can change them)
weak/non covalent- protein folding, membranes, transport, substrate binding
all amino acids have - ANS-H atom
carboxyl group
amino group
Rgroup (differentiating factor)
Linus Pauling and Robert Corey - ANS-X ray crystallography
- found alpha helix and beta pleated sheets (both interchain H bonding)
,bonds between each amino acid - ANS-peptide bond
amino acid chain= polypeptide backbone
polar and nonpolar amino acids face opp sides in backbone
electrostatic interactions - ANS-between carboxyl and amino group of different amino acids
van der waals interactions - ANS-between methyl group off of side chains
alpha helix - ANS-tightly coiled
rod arrangement of amino acids
R-grop radiates outwards
backbone is repeating units of amino group bonded to carbonyl group
(n+4 rule)
3.6 amino acids per turn
right handed
a helix cont. - ANS-two or more a helices intertwine to form coiled coil (ex. keratin, fibrin,
myosin)
hemoglobin high in a helix content
chymotrypsin lacks a helix
b pleated sheet - ANS-forms sheet by H bonding between amino and carboxyl groups of dif
peptide chains
parallel, antiparallel, mixed
extended polypeptide chains
levels of protein structure - ANS-primary- amino acid residues
secondary- alpha helix
tertiary- polypeptide chain
quaternary- assembled subunits
conservation of protein domains - ANS-humans and drosophilia share portions of the same
amino acid sequences
same protein domains can be found on different proteins
another name for protein assemblies - ANS-polymer
ex. actin filaments
covalent bonds - ANS-disulfide bonds help stabilize protein structure
non covalent bonds - ANS-mediate specificity of binding between molecules
, kinetic properties of enzymes - ANS-increase rate of biological reaction without altering reaction
equilibria
decrease activation energy of a reaction
accelerate reactions through stabilization of transition states
the enzyme active site
enzyme active site - ANS-the catalytic site is 3-d
substrates bound to enzyme by electrostatic, h bonding, van der waals forces, and hydrophobic
interactions
catalytic sites form clefts crevices - ANS-substrate bound within cleft
water excluded
nonpolar character enhances binding of substrate
enzyme substrate complex - ANS-x ray crystallography, electron microscope and
spectrophotometry
enzymes derive power by bringing in favorable substrate orientation
leonor michaelis: reaction rate increases with increasing s until vmax is achieved
saturation effect - ANS-ES complexes form until substrate saturation occurs at which point no
more substrate binding sites are available
reaction rates - ANS-enzymes increase reaction rate by decreasing activation energy
allosteric regulation - ANS-feedback inhibition
regulates levels of synthesized end product
covalent modification - ANS-atp phosphorus and water involved
phosphorylation, adenylyation
uridylylation
methylation
ADP ribosylation
proteolytic modification - ANS-digestive enzymes
proof genetic info is stored in DNA - ANS-classes of biochemicals
chromosomes believed to harbor transmissible units
chromosomes have nucleic acids as well as proteins
nucleic acids are the macromolecule that carry cellular genetic material
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