Homework Answers
Chymotryprisn results:
C-1: CSIRGKRVDLGCAATCPTVKTGVDIQCCSTDNCNPF
C-2: ITPDITSKDCPNGHVCY
C-3: PTRKRP
C-4: CDAF
C-5: TKTW
C-6: IRCF
The primary structure of the polypeptide is
N-terminus-C6-C2-C5-C4-C1-C3-C-terminus.
N’-IRCFITPDITSKDCPNGHVCYTKTWCDAFCSIRGKRVDLGCAATCPTVKTGVDIQCCSTDNCNPFPTRKRP-C’.
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Deduce the primary structure of the polypeptide described: 1) N-terminal residue analysis Result: Isoleucine 2) Protease...
Explain this question please! Name (4 ofer to the Table of Amino Acids at the beginning of the exam to help solve this problem. Polypeptide I is a 12-mer and has the following amino acid compositi...
Explain this question please!
Name (4 ofer to the Table of Amino Acids at the beginning of the exam to help solve this problem. Polypeptide I is a 12-mer and has the following amino acid composition: Ala, Arg, 2 His, Leu, 2 Lys, 2 Phe, Ser, Thr, Trp Edman degradation of I shows that its N-terminal amino acid is His. Chymotrypsin cleavage of I yields peptide fragments A-D.Trypsin cleavage of I gives peptide fragments E-G. Shown below is the amino...
Please explain each part !! Thank you !! #3. Under experimental conditions, you purify a known,...
Please explain each part !! Thank you !!
#3. Under experimental conditions, you purify a known, biologically important peptide from human tissue. To determine the overall sequence, you then digest the pure peptide with trypsin and chymotrypsin (each separately) and then use mass spectrometry to identify the following sequence fragments from the overall peptide (shown in order of relative length, not necessarily in the order in which they are assembled in the whole, natural peptide). Trypsin cleavage products: Chymotrypsin cleavage...
6. Islet amyloid polypeptide (IAPP), often called amylin, is a peptide hormone that is co-secreted with...
6. Islet amyloid polypeptide (IAPP), often called amylin, is a peptide hormone that is co-secreted with insulin from pancreatic B-cells. In combination, insulin and amylin regulate blood glucose levels. In this signaling process, amylin participates in slowing gastric emptying and promoting satiety, helping to prevent spikes in blood glucose levels. Using your knowledge of protein sequencing and proteomics, answer the questions below related to amylin. A. Islet amyloid polypeptide (IAPP, amylin) is produced by processing of a precursor protein called...
Shown is the active site if carboxypeptidase. Carboxypeptidase is a protease that works to hydrolyze the first peptide bond of a polypeptide, cleaving away the N-terminal residue from the rest of the...
Shown is the active site if carboxypeptidase. Carboxypeptidase
is a protease that works to hydrolyze the first peptide bond of a
polypeptide, cleaving away the N-terminal residue from the rest of
the chain. A substrate is shown in the diagram. The orange square
shiwn indicates the bond that will be hydrolyzed.
a) put a square around the atom that will act as a nucleophile
in the first step of the mechanism.
b) put a triangle around the atom that will...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
S Review View It, lea .--. . rrnalI1No Spac Heading 1 Heading 2 Title Subtitle Subtle Ern Emphas ...
s Review View It, lea .--. . rrnalI1No Spac Heading 1 Heading 2 Title Subtitle Subtle Ern Emphas Paragraph Styles 1. Explain how you would isolate a mixture of Ala-Arg-Glu using a negatively charged resin (carboxylmethyl cellulose) and a positively charged resin (DEAE). A sample of a peptide of unknown sequence was treated with trypsin; another sample of the same peptide was treated with chymotrypsin. The sequences (N-terminal to C-terminal) of the smaller peptides produced by trypsin digestion were 2....
In part A, yes you should reconstitute the full-length protein sequence from the fragments. However, you...
In part A, yes you should reconstitute the full-length protein
sequence from the fragments. However, you do not need to write out
the amino acid sequence - you can just provide the order of the
fragment numbers (from either set of fragments). For
example (and this is not the answer), you could say:
"Using the Pro-IAPP fragment set, starting from the N-terminus, the
fragment order is '5-4-6-3-2-1' " and that would fully address the
question.
In part B, the hint...
1. Where is the ER targeting sequence located in the polypeptide chain (N-terminal, interior, or C-terminal)...
1. Where is the ER targeting sequence located in the polypeptide chain (N-terminal, interior, or C-terminal) 2. Name 4 organelles that require organelle specific targeting sequences in polypeptide 3. Name 3 final locations for proteins with ER signal sequence 4. Satranslational translocation: (a) Name the protein that the signal sequence binds to (b) Name the protein SRP binds to 5. State the function of signal peptidase 6. Name a membrane protein that is not a single pass membrane protein 7....
1. Partial hydrolysis of lysozyme yielded an octapeptide that was later identified as the N-terminal segment of...
1. Partial hydrolysis of lysozyme yielded an octapeptide that was later identified as the N-terminal segment of the protein. From the following information, determine the sequence of this octapeptide. a. The following amino acids were identified after complete hydrolysis of the octapeptide: Arginine (Arg) Glycine (Gly) Phenylalanine (Phe) Cysteine (Cys) Leucine (Leu) Valine (Val) Glutamic Acid (Glu) Lysine (Lys) b. Treatment of the octapeptide with dinitroflurobenzene (Sanger reagent) followed by complete hydrolysis gave lysine (Lys) labeled with two dinitrophenyl (DNP) groups. c. Treatment of the octapeptide with trypsin gave lysine...
Q 4. Explain how Fig.1A (arrow) result corroborates with the author hypothesis about Parkin aggre...
Q
4. Explain how Fig.1A (arrow) result corroborates with the author
hypothesis about Parkin aggresome and proteasome activity in PD?
MG-132+ HMW 127- 84-- 41- DTT+ IP T HMW 6- IP : anti-flag WB: anti-ubiquitin Fia. 1. Parkin forms plexes A, HEK 293Tells transiently tranafected with FLAG-Parkin were divided into twe dishes and were either untreated or treated with 5PM MG-132 for 161). Cells were then lysed abidใหr-taining 1% Triton X-100 ลnd fractitated into "Iuble (S) and insoluble u) frac...
Explain this question please!
Name (4 ofer to the Table of Amino Acids at the beginning of the exam to help solve this problem. Polypeptide I is a 12-mer and has the following amino acid composition: Ala, Arg, 2 His, Leu, 2 Lys, 2 Phe, Ser, Thr, Trp Edman degradation of I shows that its N-terminal amino acid is His. Chymotrypsin cleavage of I yields peptide fragments A-D.Trypsin cleavage of I gives peptide fragments E-G. Shown below is the amino...
Please explain each part !! Thank you !!
#3. Under experimental conditions, you purify a known, biologically important peptide from human tissue. To determine the overall sequence, you then digest the pure peptide with trypsin and chymotrypsin (each separately) and then use mass spectrometry to identify the following sequence fragments from the overall peptide (shown in order of relative length, not necessarily in the order in which they are assembled in the whole, natural peptide). Trypsin cleavage products: Chymotrypsin cleavage...
6. Islet amyloid polypeptide (IAPP), often called amylin, is a peptide hormone that is co-secreted with insulin from pancreatic B-cells. In combination, insulin and amylin regulate blood glucose levels. In this signaling process, amylin participates in slowing gastric emptying and promoting satiety, helping to prevent spikes in blood glucose levels. Using your knowledge of protein sequencing and proteomics, answer the questions below related to amylin. A. Islet amyloid polypeptide (IAPP, amylin) is produced by processing of a precursor protein called...
Shown is the active site if carboxypeptidase. Carboxypeptidase
is a protease that works to hydrolyze the first peptide bond of a
polypeptide, cleaving away the N-terminal residue from the rest of
the chain. A substrate is shown in the diagram. The orange square
shiwn indicates the bond that will be hydrolyzed.
a) put a square around the atom that will act as a nucleophile
in the first step of the mechanism.
b) put a triangle around the atom that will...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
s Review View It, lea .--. . rrnalI1No Spac Heading 1 Heading 2 Title Subtitle Subtle Ern Emphas Paragraph Styles 1. Explain how you would isolate a mixture of Ala-Arg-Glu using a negatively charged resin (carboxylmethyl cellulose) and a positively charged resin (DEAE). A sample of a peptide of unknown sequence was treated with trypsin; another sample of the same peptide was treated with chymotrypsin. The sequences (N-terminal to C-terminal) of the smaller peptides produced by trypsin digestion were 2....
In part A, yes you should reconstitute the full-length protein
sequence from the fragments. However, you do not need to write out
the amino acid sequence - you can just provide the order of the
fragment numbers (from either set of fragments). For
example (and this is not the answer), you could say:
"Using the Pro-IAPP fragment set, starting from the N-terminus, the
fragment order is '5-4-6-3-2-1' " and that would fully address the
question.
In part B, the hint...
1. Where is the ER targeting sequence located in the polypeptide chain (N-terminal, interior, or C-terminal) 2. Name 4 organelles that require organelle specific targeting sequences in polypeptide 3. Name 3 final locations for proteins with ER signal sequence 4. Satranslational translocation: (a) Name the protein that the signal sequence binds to (b) Name the protein SRP binds to 5. State the function of signal peptidase 6. Name a membrane protein that is not a single pass membrane protein 7....
Q
4. Explain how Fig.1A (arrow) result corroborates with the author
hypothesis about Parkin aggresome and proteasome activity in PD?
MG-132+ HMW 127- 84-- 41- DTT+ IP T HMW 6- IP : anti-flag WB: anti-ubiquitin Fia. 1. Parkin forms plexes A, HEK 293Tells transiently tranafected with FLAG-Parkin were divided into twe dishes and were either untreated or treated with 5PM MG-132 for 161). Cells were then lysed abidใหr-taining 1% Triton X-100 ลnd fractitated into "Iuble (S) and insoluble u) frac...
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