Which of the following are not driving forces for protein folding i. Salt Bridges ii. Conformational Entropy Entropy of the Solvent iii. iv. Internal Hydrogen Bonding V. Disulfide Bonds
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- You have a mixture of 4 amino acids (Q, W, E, R, T) that you want to separate using ion exchange chromatography. Which of these amino acids would bind most strongly to a DEAE anion exchange column at pH 7? Q W E R TPart A What is the highest structural level of protein structure represented in the following image? tertiary primary secondary O pentanary O quaternary Submit Request Answer O O O OBeta-mercaptoethanol (BME) disrupts the types of interactions responsible for ____ structure of proteins. (Select all that apply!) a Primary b Secondary c Tertiary d Quaternary
- Addition of _____ to a multi-subunit protein would involve the breaking of covalent bondsa. Tween-80, a detergentb. 5.0 M NaClc. Dithioerythritold. Guanidinium hydrochloridee. None of the abovepls explain whyWhich of the following factors do not stabilize the 3-D structure of a folded protein? O Disulfide bonds O Van der Waals interactions O Hydrogen bonds O Electrostatic interactions O Hydrophobic bonds Metal-ion protein interactionsDraw the protein folding pattern when the polypeptide is immersed in water and in oil. Justify your answers by using chemical explanations. In the structure, point all possible types of intramolecular forces of attraction possible for this polypeptide in the indicated solvent system and discuss each. Discuss your answer H3N*-ala-ile-trp-arg-gly-ala-his-tyr-trp-gly-gly-tyr-arg-ile-val-thr-ile-trp-cys- met-gly-ile-asp-cys-thr-glu-cys-trp-gly-cys-phe-arg-his-pro-val-phe-CO-
- Describe in no more than ten sentences the four levels of protein structure, and cite the noncovalent force(s) in each.After carefully reviewing the material (CS links, slides, etc) complete the table about various bonds present in all four levels on proteins' conformation. You need to make a 4x4 table (see below how to make one) to put + and - signs for Yes or No. Bond types Primary Secondary Tertiary (Quaternary) Task: no response to others is needed; just post before your class. Searchentries hon Unread 12t Parrah BIVA Ev Tv v v め▼ レm 2 E Te Tale ppertie K Delete Cel Row Calum Su Search entries or author Unread 2/2 6 Reply sert delete home end prt se Tum backspace tock %23 5 T Y E enter F H K D shift C V B N pg dn pg up alt ctrl Spaced Reption. Day one- Da82 Protein levels Covalent puoq-H lonic Van der Waals1. Complete the table below with information about the amino acids utilized in this pro- cedure. Remember that smaller amino acids will travel further and so will amino acids that are soluble in the solvent. Table 9-1. Amino Acids Procedure AMINO ACIDS Phenylalanine Aspartic Acid Leucine Proline matemps DRAW THE MOLECULAR STRUCTURE in POLARITY (IS IT POLAR OR NONPOLAR?) odme her basalu la MOLECULAR WEIGHT SIZE (RANK LARGEST = 4 AND SMALLEST = 1) SHOULD IT REACT WITH NINHYDRIN?
- Lecture 2 Quiz Time limit: Length: Scor Lecture Quiz in Lecture Quizzes No time limit 10 questions 13 Time Remaining: Save Progress Last Saved: 11:45 AM Not Timed O None of the above 8) When a protein is not functional, it is said to be (1pts) N denatured O recalibrated Oallocated O tore up D All of the above O None of the above 9) Which of the following environmental conditions can alter a protein's functio that apply) O Type here to search 立Protein denaturation is the disruption of a protein's secondary to quaternary structures. Protein denaturation is always reversible. [, O The FIRST statement is TRUE. O The SECOND statement is TRUE. O BOTH statements are TRUE. O NONE of the statements are TRUE.Which of the following protein is a glycoprotein as evidenced by the provided illustration and information only? }} OI O O III =GPI Anchor OI and II II OI and III III