BSI EXAM 1 Flashcards
What helps the protein from being degraded by enzymes?
Glycosylation
What is phagocytosis?
Phagocytosis is the process by which bacteria, dead tissue, or other bits oif microscopic material are engulfed by cells
Pair of Centrioles and Pericentriolar material is called the ______
Centrosome
What is autophagy?
Autophagy is controlled digestion of damaged organelles within a cell.
This contains digestive enzymes.
Lysosomes
This is made up of cylindrical array of microtubules.
Centrioles
Glycosylation
Adding of a sugar group to the protein.
Trans face of the Golgi Apparatus faces the ER. T or F?
FALSE, The CIS face, faces the ER
Glycosylation usually happens with membrane proteins and __________.
Lipids
What is the mitotic spindle?
The mitotic spindle is the macromolecular machine that segregates chromosomes to two daughter cells during mitosis. It is made up of microtubule polymers.
Gln192 is a __ residue located 192 amino acids from the __ terminus
Glutamine; N
which of the following pairs of aa can form an ionic bond with each other
a) Lys and Glu
b) Ser and Arg
c) Gln and Lys
D) Pro and Cys
a)
What functional group is the “N-terminus”?
Amino group
If you add a chemical that breaks a noncovalent bond, what structural level is affected?
Secondary, tertiary, quaternary
Name the 10 amino acid with nonpolar side chain.
Alanine (Ala), Glycine (Gly), Valine (Val), Leucine (Leu), Isoleucine (Lle), Proline (Pro), Phenylalanine (Phe), Methionine (Met), Tryptophan (Trp), Cysteine (Cys)
T or F; Reduced form has a disulfide bond.
False, Oxidized form has disulfide bonds.
Which structures are determined by unique amino acid sequence?
Tertiary and quaternary
What are the 4 amino acids that does NOT start with the first 3 letters of their name?
Asparagine (Asn), Glutamine (Gln), Isoleucine (Ile), Tryptophan (Trp)
Which 3 amino acid contains an OH group that can be phosphorylated?
Serine (Ser), Threonine (Thr), Tyrosine (Tyr)
N-terminus, is that the beginning or the end of the protein?
Beginning
(Ser-Gln-Asn) and (Leu-Phe-Gsy), which one is more likely to be a membrane protein and why?
Leu-Phe-Gsy because it’s nonpolar and prefer membrane environment.
What functional group is the “C-terminus”?
Carboxyl Group
Adding a chemical solution to denature a protein that is in its functional quarternary structure as a heterodimer. The protein does not contain cysteine. The chemical solution interferes with noncovalent bonds. In what form would you most likely predict the protein to end up.
As two separate polypeptide chains with no secondary or tertiary structure.
T or F? A protein can only have one function
False, proteins can have multiple domains.
Name the 8 essential amino acid
Threonine, Methionine, Lysine, Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan
Define Domain
Part of the protein that can fold up on its own and have its own function.
Which amino acid contains SH and can form disulfide bonds?
Cysteine (Cys)
Name the 2 amino acid with negative side chain
Aspartic Acid (Asp) and Glutamic acid (Glu)
A polar protein that loves water and avoids lipids, would most likely be what kind of protein?
Cytosolic
Name the 5 amino acid with uncharged polar side chain
Asparagine (Asn), Glutamine (Gln), Serine (Ser), Threonine (Thr), Tyrosine (Tyr)
Name the 3 amino acid with positive side chain
Arginine (Arg), Lysine (Lys), Histidine (His)
What is the three letter abbreviation for Alanine?
Ala
What is the three letter abbreviation for Glutamic acid?
Glu
What are the 8 essential AAs?
Threonine, Methionine, Lysine, Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan
What is the three letter abbreviation for Tryptophan?
Trp
What is the three letter abbreviation for Asparagine?
Asn
What 3 AAs contain an -OH group which can be phosphorylated?
Ser, Thr, Tyr
What is the three letter abbreviation for Leucine?
Leu
What is the three letter abbreviation for Proline
Pro
What is the three letter abbreviation for Glutamine?
Gln
What is the three letter abbreviation for Histidine?
His
What is the three letter abbreviation for Serine?
Ser
What is the three letter abbreviation for Glycine?
Gly
What is the three letter abbreviation for Tyrosine
Tyr
What is the three letter abbreviation for Phenylalanine?
Phe
What is the three letter abbreviation for Valine?
Val
What is the three letter abbreviation for Isoleucine?
Ile
What 5 AAs have an uncharged polar side chain?
Asparagine (Asn), Glutamine (Gln), Serine (Ser), Threonine (Thr), Tyrosine (Tyr)
What is the three letter abbreviation for Cysteine?
Cys
What 2 Amino Acids have a negative side chain?
Aspartic acid (Asp) and Glutamic acid (Glu)
What is the three letter abbreviation for Methionine?
Met
What 3 AAs have a positive side chain?
Arginine (Arg), Lysine (Lys), and Histidine (His)
What 10 AAs have a nonpolar side chain?
Alanine (Ala), Glycine (Gly), Valine (Val), Leucine (Leu), Isoleucine (Ile), Proline (Pro), Phenylalinine (Phe), Methionine (Met), Tryptophan (Trp), Cysteine (Cys)
What is the three letter abbreviation for Threonine?
Thr
What is the three letter abbreviation for Lysine?
Lys
What is the three letter abbreviation for Aspartic acid?
Asp
What is the three letter abbreviation for Arginine?
Arg
What recognizes tag (chain of ubiquitin) and degrades the protein?
Proteasome
Degraded proteins are turned back into ____________
peptides
Covalent bonds are the type of bonds that holds the ligand in binding site.
False, noncovalent bonds.
Define: Denaturation
The process in which a protein loses its quaternary, tertiary, and secondary structure present in their native state.
What is a small molecule that functions as a transient carrier of a functional group?
Coenzyme
What enzyme recognizes specific degradation signals on proteins and then adds a chain of ubiquitin?
Ubiquitin ligases.
What is the first step in the UPS?
Protein is tagged with ubiquitin.
What is disrupted during denaturation.
Nonconvalent bonds maintaining secondary, tertiary, and quaternary structure.
INCORRECT