problem set 8 Flashcards
LACKS conversion between IE and pH changes
NO chiral carbons
glycine
Two chiral carbons
isoleucine
threonine
at a pH of 9.7 alaine
-1
at a pH of 9.7 glutamic acid
-2
at a pH of 9.7
lysine
0
at a pH of 9.7
alanine, glutamic acid, lysine
-positive electrode-
move to the positive electrode
at a pH of 9.7
alanine, glutamic acid, lysine
-negative electrode-
none
at a pH of 9.7
alanine, glutamic acid, lysine
-don’t move-
lysine
pH 9 the protein would have a ____
negative charge
pH 4 it would have __
positive charge
proteins are least soluble
at their isoelectric point
when the isoelectric points are negative
they move to the positive electrode
changes in the pH most affect what type of bonding in proteins
ionic interactions (salt bridges)
polypeptides with few acid or basic side chain amino acids are less sensitive to pH changes than polypeptides with a higher number of side chains
the acid and basic side chains are in the salt bridge
polypeptides with few acid and basic side chains have very few salt bridges
thus they are not sensitive to pH change
what type of bonding is found in the primary structure of proteins
amide bond
amide bond is the same as a peptide linkage
what type of bonding is NOT found between protein chains in the quaternary structure
hydrophobic interactions
hydrophobic amino acid side chains are mostly found in the inside of a globular protein
hydrogen bonding of “O” in the amide and the “H from the nitrogen backbone
2
more than one polypeptide chain linked together
4
alpha helix
2
triple helix
4
slat bridges within a chain
3
hydrophobic interactions
3
disulfide bonding between chains
3
amino acid sequencing
1
beta sheets
2
albumin
Globular proteins
myosin
Fiberous proteins
collagen
Fiberous proteins
hemoglobin
Globular proteins
wool
Fiberous proteins
myoglobin
Globular proteins
silk
Fiberous proteins
serum globulins
Globular proteins
proteins used for structure
Fiberous proteins
proteins used for transportation
Globular proteins
proteins used for catalyzing reactions
Globular proteins
proteins used of muscle contraction
Fiberous proteins
Fiberous proteins
are used for structure
Globular proteins
are fragile
used for enzymes and transportation
which are most easily denatured
fiberous or globular proteins
globular proteins are easily denatured
which has a greater solubility in aqueous solution, fibrous or globular protein
globular proteins are much more soluble than fiberous protiens
fiberous proteins are used for structural purposes
how many poplypeptide chains are in:
myoglobin
1 chain
how many poplypeptide chains are in:
hemoglobin
4 chains
how many poplypeptide chains are in:
immunoglobulin
4 chains
how many poplypeptide chains are in:
collagen
3 interwoven chains
in a globular protein which amino acids would probably be found exclusively in the inside of the protein
Phenylalanine
Tryptophan
Glycine
which protein is replaced the most often
enzymes
which protein is replaced the least often
collagen
threonine
serine
Hyrogen bonding
valine
alanine
Hydrophobic interaction
arginine
aspartic acid
salt linkages
lysine
lysine
hydrogen bonding
two cysteines
disulfide bonds
arginine
glutamic acid
salt linkages
phenylaline
isoleucine
hydrophobic interaction
tyrosine
lysine
hydrogen bonding
lysine
glutamic acid
salt bridge
asparagine
lysine
hydrogen bonding
glutamic acid
aspartic acid
hydrogen bonding
arginine
tyrosine
hydrogen bonding
aspartic acid
lysine
salt linkages
phyenylalanine
alanine
hydrophobic interaction
serine
lysine
hydrogen bonding
tyrosine
glutamine
hydrogen bonding
leucine
valine
hydrophobic interaction
what amino acids have side chains that can help form salt bridges
glutamic acid or aspartic acid
with lysine or arginine
transports oxygen in blood
hemoglobin
destroys invading bacteria by breaking down its cell walls
lysozymes
protein in silk
fibroin
muscle protein used for movement
myosin
stores oxygen in heart muscles
myoglobin
hormone which regulates glucose metabolism
insulin
antibody (combats infection)
immunoglobin
protein in bone, connective tissue
collagen
stores iron in the spleen
ferritin
protein found in ligaments
elastin
protein involved in blood clotting
thrombin
protein that transports fatty acids
serum albumin
polypeptide involved with water retention
vasopressin
milk protein
casein
protein in hair, nails, hooves
keratin
blood protein which regulates osmotic pressure
serum albumin
protein found in elastic tissue in artery wall
elastin
poly peptide involved with lactation and induction of labor
oxytocin
the fibrous protein which is very strong because of its triple helix structure
collagen
the protein found in HDL or LDL
serum globulins
most abundant protein in the human body
collagen
proteins are least soluble at their isoelectric points. what would happen if a few drops of HCL were added to a protein which was already precipitated at is isoelectric point
the protein would begin to dissolve because the charges on the amino acid side chains would change. there would be more postivie charges than negative charges