You are studying Protein A. In the picture below, which location is Protein A MOST likely to move to, and which location is Protein A LEAST likely to move to? 3 4 Protein A 1 2
Q: Consider what would happen if you had a pure preparation of each of the substances below, which you…
A: There are four classes of biological macromolecules: nucleic acid, lipids, carbohydrates and…
Q: People are very interested in understanding how prions fold. (Prions are proteins that begin…
A: 1. To determine which protein, mouse or bovine, will be more "folded" at 310K, we need to compare…
Q: 2. An enzyme-catalyzed reaction has a Km = 120 μM. At what substrate concentration would this…
A: In enzyme kinetics, the Michaelis-Menten constant, or Km, is a parameter that characterises the…
Q: You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts…
A: S to P conversion is said to have a of -6 kJ/mol. So, let's give 'S' a free energy (G) value of 0…
Q: Polysaccharides Monosaccharides, Disaccharides and Polysaccharides Monosaccharides and Disaccharides…
A: Functional carbohydrates are essential for providing energy, maintaining blood sugar levels, and…
Q: 2.(a) The two diagrams on the right compare O2 binding pro- perties of Hb Kariya, a human hemo-…
A: Here we are given the hill plot for analyzing the binding kinetics of 2 hemoglobin (Hb) variants,…
Q: When transaminated, the three branched-chain amino acids (valine, leucine, and isoleucine) form…
A: Maple syrup urine disease is caused by a deficiency in the branched-chain α-keto acid dehydrogenase…
Q: We humans do not express an alpha-Galactosidase enzyme and therefore cannot break down stachyose but…
A: Stachyose is a tetrasaccharide made up of two , one and one . Stachyose can be represented as .Gal…
Q: Identify the species that are liganded to the porphyrin ring Fe(II) ion in deoxyhemoglobin (i.e., Hb…
A: The protein haemoglobin, which is present in red blood cells, is essential for the movement of…
Q: In the absence of an enzyme, a reaction has a Keq = 10¹5. i. Is AGO for the reaction + or -? ii.…
A: In a general reaction such as:aA + bB ⇌ cC + dDAt equilibrium (steady state), the concentration of…
Q: Assume that the complete combustion of one mole of fructose, a monosaccharide, to carbon dioxide and…
A: ∆G°' = -2810 kJ/mol∆G°'compound x = -38.1 kJ/mol Moles =?
Q: When the blood passes through the lungs, CO₂ is expelled and the hemoglobin picks up oxygen. Place…
A: In the process of oxygenation of hemoglobin in the lungs and the release of carbon dioxide, certain…
Q: Which of the following runs an identical application as the production environment? Select one: Oa.…
A: The natural world that hosts living things is known as the environment. It consists of the…
Q: What might happen to someone if their cells no longer recognized ghrelin's message? they would never…
A: Ghrelin is a hormone produced mainly by the stomach and, to a lesser extent, by other tissues in the…
Q: why are lysozyme and ovoalbumin the recommended standards used in the Bradford protein assay and why…
A: Lysozyme is an enzyme found in tears, saliva and mucus which plays a role in destroying bacterial…
Q: What are the main products of anaerobic glycolysis? Hoe does each one get metabolized?
A: Anaerobic glycolysis is defined as a metabolic process which takes place when oxygen is not present…
Q: PEGylation plays an important role in the formulation of nanoparticle-based therapeutics: mark all…
A: PEGylation is a process in which polyethylene glycol (PEG) molecules are covalently attached to…
Q: DNA sometimes has chemical groups attached, called methyl groups, that affect gene expression.…
A: Methyl groups on DNA have a significant role in epigenetics and gene regulation and have a strong…
Q: G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) are two basic receptor…
A: GPCR stands for G Protein-Coupled Receptor a type of cell surface receptor involved in signaling.RTK…
Q: 15. Write the metabolites of the following substrates due to phase Il reactions: a. b, R R C. R 20 R…
A: Enzymes are proteins that catalyse biochemical reactions. Enzymes sometimes require a non-protein…
Q: How many co2 are produced from 1 glucose and 1 c16 fatty acid?
A: During the process of cellular respiration, one glucose molecule breaks down into six carbon dioxide…
Q: The protein fragments ABS1 and ABS2 of tropomodulin were produced as fusion proteins with chitin…
A: It is possible to filter proteins or fragments of proteins which have been fused with a…
Q: The C-2 epimer of A is [Select] [Select] H- Н- НО Н- -H CHO OH OH Н H OH НО НО OH -H -H Н- Н- CHO B…
A: Carbohydrates are polyhydroxy aldehydes or ketones. Monosaccharides are simplest carbohydrates:…
Q: Briefly list out the chemicals contributing the anti-oxidative activities found in green tea.
A: Green tea is the most widely consumed beverage, following water.The chemicals present in green tea…
Q: Monosaccharides can be classified based on the number of carbons they contain and the type of group…
A: The most basic type of carbohydrates are called monosaccharides, or "simple sugars." They are made…
Q: 2. NAD is synthesized from the vitamin niacin. The daily dietary intake of niacin recommended for…
A: NAD' is synthesized from the vitamin niacin. The daily dietary intake of niacin recommended for…
Q: The activity of chymotrypsin changes as the pH changes in the range of pH 5-9, as shown on the a.…
A: Chymotrypsin is an enzyme that aids in breaking down proteins within the body. It is produced by the…
Q: In the article the authors reference the canonical forces in protein folding. Describe how these…
A: As per the central dogma of molecular biology, the DNA contain the information needed to synthesize…
Q: Dimethoate is a commonly used agrochemical. However, chronic exposure to it can cause an individual…
A: Hyper-ß-alaninemia is a condition characterized by excessive alanine in the muscles. In the context…
Q: Which of the following will result from the binding of one O₂ to a molecule of hemoglobin? the…
A: When one molecule of oxygen (O2) binds to a molecule of hemoglobin, it triggers specific…
Q: Single stranded DNA fragment of M13 phage DNA shown was mixed with the following primers P1: AGTAG…
A: Polymerase chain reaction also abbreviated as PCR.A specific DNA fragment is quickly multiplied…
Q: The approximate thickness of the phospholipid bilayer is 10A 1 micro M 50A 150A 1nM
A: There are four classes of biological macromolecules - nucleic acid, proteins, lipids and…
Q: In N-linked glycoproteins, the sugar molecule is usually bound to Thr Asn Asp Ser
A: N-linked glycoproteins are proteins that have sugar molecules specifically oligosaccharides attached…
Q: Which of the following are roles of the distal histidine in hemoglobin? to help to keep the heme in…
A: The distal histidine in hemoglobin plays a crucial role in its functioning. Let's analyze the…
Q: There is another melanocyte-stimulating hormone called B-melanotropin. Cleavage of 3-melanotropin…
A: We have find out the sequence of amino acids
Q: Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to…
A: Proteases are enzymes that cleave peptide bonds that link two amino acid residues together.…
Q: select the false statement regarding phospholipid bilayer membranes. phospholipid bilayer part…
A: A cell is made up of different biomolecules. Biomolecules are of four types: carbohydrates,…
Q: Skull parts are represented in only of the more than 100 genera of sauropods. (A) 20 (B) 24 36 (D)…
A: Answer :- The vast, herbivorous sauropod dinosaurs, which flourished during the Mesozoic Era, are…
Q: Which of the following is not a CYP450 catalyzed oxidation/reduction reaction? O A. deamination OB.…
A: The Cytochrome P450 (CYP450) enzymes are a group of enzymes that play a crucial role in the…
Q: 3. Fates of pyruvate. Pyruvate has several metabolic fates (some of which you'll learn later) but in…
A: Pyruvate is an important product of glycolysis. It can also be defined as an important junction…
Q: Frog muscle cells and the solution bathing the cells contain ions at different concentrations. The…
A: The concentrations of Na+, Ca2+, K+, and Cl- are shown in the following table. Temperature = 25…
Q: What are the differences in atp formation in glycolysis vs oxidative met
A: ATP (adenosine triphosphate) is a critical molecule that stores and releases energy for cellular…
Q: 1. The figure below shows the ribosome elongation cycle in translation. Label the features indicated…
A: Translation is the process by which a polypeptide chain is synthesized based on the information…
Q: R dy O -D 117 9, 1811 5 96 OF fa -Only-
A: Answer :- A vital physiological mechanism that aids in keeping our blood's pH within a certain and…
Q: Which of the following statements regarding the ends of polysaccharides are true? 1) All…
A: Polysaccharides are polymers of monosaccharides. Multiple monosaccharides get bonded to each other…
Q: Why might the compound below be a potent transition state analog inhibitor for isocitrate…
A: Transition states are short-lived species that arise as a substrate is being converted to a product…
Q: 1. Start with the Michaelis-Menten equation and convert it to a double-reciprocal equation. Show how…
A: For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…
Q: Match the colour of myoglobin to the ligand bound. brown red pink 1. carbon monoxide 2. nitric oxide…
A: Muscle tissue contains a protein called myoglobin, which is essential for storing and transferring…
Q: 3. Now for the citric acid cycle, it is time to follow the carbons! Using labeled pyruvate:…
A: Citric acid cycle is a metabolic pathway that regenerates oxaloacetate from citrate. Acetyl CoA from…
Q: Which of the following statements is WRONG with regard to the following molecule?
A: A cell is the basic structural and functional unit of life where all the metabolic activities are…
Step by step
Solved in 3 steps
- VITATI KEY: Positive charge: Purple, Negative Charge: Pink Hydrophilic: Green Hydrophobic: Brown MOSTU. TOUT um b. Now change the second pull down to oil. What changes? וועען a. Set the first pull down to show charge and hydrophobicity and the second pull down as water. Click generate random protein, and then select random mix (last option). Run the simulation (arrow in center of playbar). What do you notice? (ie What type of amino acid are on the outside?) When you run it again, what is the same and what is different? c. Now change the second pull down to vacuum. What changes? What type of interactions remain? d. Now instead of ‘random mix’, click Mostly hydrophobic and toggle between oil and water. What do you notice? e. Lastly click All hydrophilic and toggle between oil and water. What do you notice? 2. What are the monomers (one subunit) of a polypeptide called? ● On the left half of the space below, draw a simple structure of a protein monomer with uncharged functional groups and…6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.6a. Using your 5 mg/mL stock solution, you wish to make 100µL of the correct concentration of protein to load. How do you make this working solution? (Yes- you would want this to be in 1x sample buffer, but that makes this question more complicated. So for this question just make the protein in water.) Volume of 10mg/ml Final Volume ! 1 100μL of protein 6b. This is a 1: A N Body* @ 2 W S dilution. #3 X E D $ 4 A C R F B I % 5 T V MacBook Pro U וכ H E U 8 N J ( 0
- Help me3. A. Briefly discuss the four levels of structure in proteins. Knowing that the 3-dimensional shape of a protein is important to its function, discuss on a qualitative basis whether the changes below will likely alter the function of a protein, justifying your answer with why or why not. B. What would happen to a protein's functionality if a serine residue were replaced with threonine? C. What would happen if serine were replaced with leucine? D. What would happen if serine were replaced with cysteine? E. What would happen if aspartic acid were replaced with tryptophan in the part of the protein (an enzyme) that serves as an active site to catalyze a reaction? F. What would happen if aspartic acid were replaced with tryptophan in a non-active site?Which of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..
- Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (c) Outline how you would investigate whether BCMAP would be an effective inhibitor for the protein in competition with the molecules that the protein normally targets, and any solvent. Figure 1. 4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and brown, respectively) in the active site of the protein structure.. Theoretical and experimental measurements show that in many cases, the contributions of ionic and hydrogen-bonding interactions to AH for protein folding are close to zero. Provide an explanation for this result.,2 If a protein is predominantly made up of aliphatic and aromatic amino acids, which of the following is most likely true about such protein? Select the correct responses): a. It is a protein with a net negative charge b. It is most probably a structural protein. c. It is a protein that is cationic in nature. d. It is a protein that is hydrophobic in nature. e. It is most probably a catalytic protein. f. It is a water-solube protein. g. It is most probably a carrier protein.
- Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.Which of the following statements about protein folding and structure are true? Check all that apply. Chaperones, like the GroEL-ES complex, work by providing a sequestered environment in which proteins can safely explore the conformational space towards productive folding. O Chaperones "know" how to actively fold proteins into their proper final structure. Each protein has its own "assigned" chaperone to assist in its proper folding. O Misfolded proteins are innocuous and readily cleared by the cell. V The native structure of a protein is entirely encoded in its amino acid sequence. Misfolded proteins often aggregate in large structures in the cell. Misfolded proteins are thermodynamically stable versions of a protein.Consider five proteins with the properties shown in the following table. Answer the questions below about these proteins and justify your answers. Protein Subunit mass (Da) | Native mass (Da) 10,000 40,000 120,000 A 15,000 C 20,000 20,000 25,000 75,000 E 30,000 60,000 a) Which protein would migrate the slowest in an SDS-PAGE? Justify your results. b) Which protein would migrate the fast in a Native-PAGE? Justify your results.