latch the following examples with the levels of protein structures. 4 1 2 3 > < > > The overall fold of a hemoglobin tetramer The arrangement of tour helices in E. coli cytochrome b x-helices, B-sheets, Q- loops Collagen Lys- His-Arg-Arg-Cys-Ala- Gly-Leu 1. Primary Structure 2. Secondary Structure 3. Tertiary Structure 4. Quaternary Structure
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- Which of these statements about hemoglobin is NOT true? A) it is a tetrameric globular protein b) it has a prosthetic group called heme c) it’s dominant motif is beta barrel d) its dominant motif is helix-turn-helix The reagent used to break disulfide bonds is: a) urea b) beta-mercaptoethanol c) guanidine hydrochloride d) phosphorus pentachloridewhat are the structural features of the protein 6VJI? primary , secondary What are two features of 6VJI's What are two features of your protein’s structure that make it different or similar to haemoglobin are two features of your protein’s structure that make it different or similar to haemoglobin? structure that make it different or similar to haemoglobin?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..
- For each of the following amino acids: 1) describe what the important functional group of the amino acid side chain is, 2) identify the charge of the side chain, 3) name another component in the structure that the amino acid might interact with, and 4) indicate how the interaction with the component listed in 3) might be occurring (i.e., electrostatic interaction, hydrogen bond, hydrophobic interaction, etc.) a) Asp153 b) Arg166 c) Lys167A particular amino acid contains a -CH2NH3+ group. Is this amino acid more likely to be found on the inside or outside of the folded protein? Briefly explain.Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
- Rationalize the following observations.(a) Serine is the amino acid residue that can be replaced with theleast effect on protein structure and function.(b) Replacement of tryptophan causes the greatest effect on protein structure and function.(c) Replacements such as Lys -> Arg and Leu -> Ile usually havevery little effect on protein structure and function.Take a look at the multiple-sequence alignment shown ofthe globin polypeptides, focusing on amino acids 101 to 148.A. Which of these amino acids are likely to be most important forglobin structure and function? Explain why.B. Which are likely to be least important?how do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...
- Consider the following peptide sequence: Lys-Leu-Ile-Cys-Lys What is the net charge of this sequence at physiological pH? a. -2 b. +1 c. 0 d. -1 e. +2In the protein denaturation experiment, which of the following can be a consequence of the air bubbles in the viscometry run for an aqueous solution of protein with a denaturant?a. Increased t0b. Decreased t0c. Increased nspd. Decreased nspAll of the statements about protein denaturation are true EXCEPT:a. The viscosity of linear proteins is greater than that of the globular proteins.b. Only the BME can disrupt a covalent bond while the other denaturants can just disrupt non-covalent bonds.c. Protein renaturation is possible but in some cases protein denaturation proceeds to protein degradation. d. Protein denaturation generally disrupts tertiary or quaternary structures onlyCalculate the overall net charge of the following polypeptide at pH = 2.0Gly-Pro-Glu-Asp-Leu-His-Ile-Gln-Asn-Phe A) +1.76 B) -1.76 C) +0.24 D) -0.24