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Proteins
We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.
Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
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- The peptlde bradykinln is a nonapeptlde. Give the name of the peptide (shown below) by namlng the amlno aclds from the N-terminal to the C- terminal. Use the long name, the 3-letter abbreviation and the 1-letter abbreviation. What is the pl of this peptide? Name Compositon Fxnction LOcalizatio Bradykinl Inflammatio Different n and H N vasodilation Cells HNH n Animal H. HNH H NH он HN N HO1. Using an arrow, draw the site of cleavagr for the following peptides that are reacted by: Pepsin (a- b), trypsin (c-d), and chymotrypsin (e). H H H H H NH2 а. PEPTIDE VPQFAGI H H HN, H b. PEPTIDE DLIPAE .....H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
- 5) Explain the synthesis, release and pharmacology of histamineSubjecting this peptide to one cycle of the Edman degradation would result in L-M-F-V-W-E-Q-A-P-S-P Leucine OA. O B. Proline oc Leucine phenylthiohydantoin OD. Proline phenylthiohydantoin None of the above OE.Subjecting this peptide to trypsin would result in L-M-F-V-W-E-Q-A-P-S-P O A. Lys and Met-Phe-Val-Trp-Glu-Gln-Arg and Pro-Ser-Pro OB, Leu-Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro Leu and Met-Phe-Val-Trp-Glu-Gln-Arg-Pro-Ser-Pro OC. Op. Lys and Met-Phe-Val-Trp-Glu-Gln-Ala-Pro-Ser-Pro Leu and Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro OE.
- Given the peptide Lys-Glu-Trp a) Draw the appropriate titration curve for this peptide. Label X and Y axis b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net chargeThree polypeptides, the sequences of which are represented using the one-letter code for their amino acids, are present in a mixture: Peptide 1: ATKNRASCLVPKHGALMFWRHKQLVSDPILQKRQHILVCRNAAG Peptide 2: GPYFGDEPLDVHDEPEEG Peptide 3: PHLLSAWKGMEGVGKSQSFAALIVILA Determine which peptide would migrate most slowly during the given methods of chromatography. anion exchange chromatography Answer Bank Peptide 1 Peptide 2 Peptide 3 cation exchange chromatography size-exclusion (gel-filtration) chromatography5) Snake venom surprisingly has been a found to be a rich source of biologically active peptides. One important class of peptides includes the bradykinin potentiating peptides which were the precursors to today's most commonly used antihypertensive drugs such as captopril or lisinopril. Let's say that you are investigating a new peptide in the bradykinin potentiating peptide class from Agkistrodon bilineatus (Mexican pit viper) venom. You suspect that the peptide has the following sequence: QWAQGRAPHPP After some harrowing experiments, you've collected and isolated a sample of this peptide. How will you confirm that the sequence is what you expected? Describe a sequence of chemical tests (at least 4) that you can do on this peptide that should give you enough information to deduce the sequence. Be sure to describe in detail each of the chemical analyses and the expected results of each.
- You have isolated this peptide. AÇQGRKSPWTT TAHEVYPGGČMN What products would you get if you treated with: a) DTT ( dithiothreitol) b) Trypsin c) Carboxypeptidase A ( 1 cycle) d) Aminopeptidase M ( 2 cycles) e) DTT, then Iodoacetate, then elastaseDraw the products of the reaction of this peptide with trypsin.1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?