drexel bio 209 final EXAM fully solved & updated
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bail bonds RBT Exam practice RBT Practice Exam - 85 questions Pearso
62 terms Teacher 167 terms 84 terms 150 term
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Terms in this set (237)
weak interactions electrostatic
h bonding
van der waals
hydrophobic effect- tendency of non polar molecules to avoid contact with water
in aqueous solutions
chemical bonds strong- covalent ( enzymes can change them)
weak/non covalent- protein folding, membranes, transport, substrate binding
neg side chain amino acids apartic acid(Asp-D)
glutamic acid (Glu-E)
positive side chain amino acids Arginine(Arg-R)
Lysine (Lys-K)
Histidine (His-H)
uncharged polar side chain Asparagine (Asn-N)
Glutamine (Gln-Q)
Serine (Ser-S)
Threosine (Thr-T)
Tyrosine (Tyr-Y)
, nonpolar amino acids alanine (ala- A)
glycine (gly-G)
valine (val-V)
leucine (leu-L)
isoleucine (ile-I)
proline (pro-P)
phenylalanine (phe-F)
methionine (met- M)
tryptophan (trp-W)
cytesine (cys-C)
all amino acids have H atom
carboxyl group
amino group
Rgroup (differentiating factor)
Linus Pauling and Robert Corey X ray crystallography
- found alpha helix and beta pleated sheets (both interchain H bonding)
bonds between each amino acid peptide bond
amino acid chain= polypeptide backbone
polar and nonpolar amino acids face opp sides in backbone
electrostatic interactions between carboxyl and amino group of different amino acids
van der waals interactions between methyl group off of side chains
alpha helix 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. 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 forms sheet by H bonding between amino and carboxyl groups of dif peptide
chains
parallel, antiparallel, mixed
extended polypeptide chains
levels of protein structure primary- amino acid residues
secondary- alpha helix
tertiary- polypeptide chain
quaternary- assembled subunits
conservation of protein domains humans and drosophilia share portions of the same amino acid sequences
same protein domains can be found on different proteins
2026(latest version verified for accuracy) | 2026 Latest!!
Leave the first rating
Save
Students also studied
bail bonds RBT Exam practice RBT Practice Exam - 85 questions Pearso
62 terms Teacher 167 terms 84 terms 150 term
overkillfl Preview cherie203 Preview beccaerick18 Preview kay
Terms in this set (237)
weak interactions electrostatic
h bonding
van der waals
hydrophobic effect- tendency of non polar molecules to avoid contact with water
in aqueous solutions
chemical bonds strong- covalent ( enzymes can change them)
weak/non covalent- protein folding, membranes, transport, substrate binding
neg side chain amino acids apartic acid(Asp-D)
glutamic acid (Glu-E)
positive side chain amino acids Arginine(Arg-R)
Lysine (Lys-K)
Histidine (His-H)
uncharged polar side chain Asparagine (Asn-N)
Glutamine (Gln-Q)
Serine (Ser-S)
Threosine (Thr-T)
Tyrosine (Tyr-Y)
, nonpolar amino acids alanine (ala- A)
glycine (gly-G)
valine (val-V)
leucine (leu-L)
isoleucine (ile-I)
proline (pro-P)
phenylalanine (phe-F)
methionine (met- M)
tryptophan (trp-W)
cytesine (cys-C)
all amino acids have H atom
carboxyl group
amino group
Rgroup (differentiating factor)
Linus Pauling and Robert Corey X ray crystallography
- found alpha helix and beta pleated sheets (both interchain H bonding)
bonds between each amino acid peptide bond
amino acid chain= polypeptide backbone
polar and nonpolar amino acids face opp sides in backbone
electrostatic interactions between carboxyl and amino group of different amino acids
van der waals interactions between methyl group off of side chains
alpha helix 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. 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 forms sheet by H bonding between amino and carboxyl groups of dif peptide
chains
parallel, antiparallel, mixed
extended polypeptide chains
levels of protein structure primary- amino acid residues
secondary- alpha helix
tertiary- polypeptide chain
quaternary- assembled subunits
conservation of protein domains humans and drosophilia share portions of the same amino acid sequences
same protein domains can be found on different proteins
