Problem_Set_3

Question: What is the isoelectric point of Cysteine ​​and Glutamate, Illustrate structures and net charges (Determine the isoelectric point based on the pka) please give clear handwritten answer!

Question:- Alpha-endorphin is a peptide with an amino acid sequence of YGGFMTSEKSQTPLVT. How many charges does it have at pH 7?

Please help with part a and b both the questions urgently within an hour

Kk.83.

Materials - 2021FA-CHM-1O X Bb 4427577 d-fleet02-xythos.content.blackboardcdn.com/6086c260d7e8f/4427577?X-Blackboard-Expiration=1633143600000&X-Blackboard-Sig 6 / 9 100% Exercise 1: Standard Curve for Protein Measurements: A standard curve for protein concentration is often created using known concentrations of bovine serum albumin (protein). This process is called the Bradford Assay; it is a colorimetric assay. A special reagent turns blue when it binds to amino acids present in protein. The intensity of the color is best measured with a spectrophotometer (a device for comparing two light radiations, wavelength by wavelength). In the case of the Bradford Assay the greater the absorbance, the higher the protein concentration. A series of tests were performed on some samples and spectrophotometer: following measurements were obtained using a Protein Concentration (mg/ml) Absorbance (A) 0.26 0.098 0.56 0.213 0.383 0.84 1.12 0.473 1.40 0.527 TASKS: 1. Enter the data into Excel - the…

Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG

Question: What is the thermodynamic driving force behind the formation of a peptide bond and how does it relate to the properties of the amino acid residues involved?

Question: A decapeptide composed of ser, ala, IIe. his, trp, phe was treated with 1-flouro- 2,4-dinitrobenzene. It gave a DNP-his on the N terminal and free trp when treated with carboxypeptidase. Upon partial hydrolysis of the peptide, the following fragments were obtained. a. his-lle-phe-ala c. his-ala-phe e. ser-lle-his b. ala-phe-trp d. phe-ala-ser Give the amino acid sequence of the above decapeptide.

Question:- Explain why withholding galactose from the diet of galactosaemia patients has no effects on their synthesis of glycoprotein.

08:24 Tue Nov 23 90% T + : E) 10.0 5. A protease binds its substrate in an extended conformation for better access to its amide linkages for hydrolysis. When this happened, which quadrant of a Ramachandran plot will the substrate's phi-psi bonds most likely be located in? 180 120 60 -60 -120 -180 -180 180 6 (dearees) A) Southwest quadrant where y = negative and O = B) Southeast quadrant where y = negative and 0 = positive C) Northwest quadrant where = positive and 0 = negative D) Northeast quadrant where y = positive and O = positive E) In the center where O = ) =0° negative %3D %3D 3 %3D 22 6. Secondary structure is largely stabilized by hydrogen bonds ; tertiary structure is largely stabilized by the hydropnobic etlect. (WRITE your answer for BOTH blanks into the blanks above or in order on your answer sheet. Both must be correct for credit.) > ý (degrees)

Explain the advantage of using Fluorescence Recovery After Photobleaching (FRAP) in determining protein localisation I notes = Notes Comments MAY 7.

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Study problem 2 4. A coworker has just isolated a copper enzyme that catalyzes the conversion of oil sludge into soluble alcohols in the presence of O₂. There are two Cu atoms per protein, which consists of a single polypeptide chain. As the bioinorganic chemist on the project, you are given unlimited quantities of the protein for the purpose of determining the active site structure. You have at your disposal a number of physical techniques, including NMR and EPR spectrometers, a magnetic susceptometer, a Mössbauer instrument, an X-ray absorption beam line, a UV-VIS spectrophotometer, a Raman spectrometer, a magnetic circular dichroism instrument, but, alas, no X-ray diffractometer. You have time to complete measurements by only three techniques before you have to give a report to your colleague. Describe what measurements you would make, in what order you would make them to get the most out of time, what results you might expect, and how you would use this information to characterize…

Problem 1 Draw the twenty canonical amino acids (encoded in biological proteins) as they would appear at pH = 7, including stereochemistry found in encoded proteins. Next to each amino acid, give its name and both its 3- letter and 1-letter identifications.

Can I have help with number 2 and 3? 2) 2What is the specific function of the enzyme catalase? 3) Catalase is an enzyme found in aerobic cells. What does this mean?

Time remaining: 00:08:55 Chemistry Consider a peptide with the following amino acid sequence: H2N-ASENHLDGCPYTKSRG-COOH Analyze the predominate protonation state and thus dominate charge (+1, 0, -1) of the residues in this peptide at pH 3, 6, and 10 by filling in the table below, identifying the relevant pKa appropriate for each residue. (Note that choice of pKa and its. application will be graded independently; e.g., if you can choose the wrong pKa but apply it correctly, you will lose points only for the pKa.) AA Residue pKa Charge pH 3 Charge pH 6 Charge pH 10 A         S         E         N         H         L         D         G         C         P         Y         T         K         S         R         G

Question in photo

Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?

State True or False with explanation

2-89 The following is a block diagram for a sphingoglycolipid where the building blocks are labeled with letters and the linkages between building blocks are labeled with numbers. A 1 2 B C a. Which building blocks are fatty acid residues? b. Which building blocks are carbohydrate residues? c. Which linkages are amide linkages? d. Which linkages could involve a monosaccharide?

Question:- What biological rationale can explain why there are so few variants observed at position 65 of the heme distal ligand and position 94 of the heme proximal ligand of myoglobin? Why does the number of variants differ between the two sites?

Please answer 1 and 2

topic: Bradford AssayThere are numerous methods of protein determination in use, but this module focuses on the Bradford assay.The Bradford assay is a dye-binding method that employs Coomassie Brilliant Blue G-250, whose structureis shown in Figure 2.3.4.1. Coomassie Brilliant Blue G-250 is a dye that interacts with proteins throughhydrophobic and electrostatic interactions.     What are the identities and functions of the components of the Bradford reagent in protein contentdetermination?

1:55 .ll 0.52 KB/S 56 1.pdf CHEM 3141: BioChemistry Quiz no. 1- Answer key I.) Draw the following compounds. 1.) Maltose: 2 Glucose, a-(1,4) 2.) Gentobiose: 2 Glucose, B-(1,6) 3.) C-2 epimer of Talose 4.) C-3 epimer of Fructose 5.) C-2 epimer of ribose II. Predict the products of the following reactions, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow он FO HO -H H -OH но. + Resorcinol/dilute HCI 1.) 2.) Sucrose + Copper (II) Acetate/Acetic Acid HO H HO H HO H H OH 3.) HO + Orcinol/HCI

biochemistry

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Can you help me?

State True or False with explanation

22-A. Consider a chromatography experiment in which two compo- nents with retention factors k, = 4.00 and k2 = 5.00 are injected into a column with N = 1.00 × 10° theoretical plates. The retention time for the less-retained component is t,1 = 10.0 min. (a) Calculate fm and 1,2. Find w12 (width at half-height) and w (width at the base) for each peak. (b) Using graph paper, sketch the chromatogram analogous to Figure 22-7, supposing that the two peaks have the same amplitude (height). Draw the half-widths accurately.

Reminder : ONLY ONE GRAPH