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- D raw the full structure of the following tetrapeptide . Label the N terminaland C terminal residues. Phe - Cys - Ser - Ilec. In lab, you recorded a UV-Vis spectrum of a mixture of proteins. What best explains why two major peaks were observed in your spectrum between 240 and 480 nm? i. Amino acids absorb light at two wavelengths depending on their identity. The sample was impure. All proteins absorb light at 280 due to the presence of aromatic amino acids and red proteins absorb light near 400 nm. The buffer absorbs light in the visible region and the proteins absorb light in the UV region of the spectrum. None of the above. ii. iii. iv. V. d. In lab, you ran an SDS-PAGE gel. What best explains the importance of adding SDS and heating your samples? i. SDS is a dye used for visualization and heat is used to dissolve the SDS in solution. iii. iv. SDS coats the protein with negative charge and heat aids in the unfolding of the proteins. SDS and heat both help stabilize the proteins during gel electrophoresis. SDS and heat both help break the peptide bonds of proteins, which is necessary for gel…Arrange the following terms in order of increasing specialization: oligopotency, pleuripotency, unipotency, multipotency. multipotency, pleuripotency, oligopotency, unipotency pleuripotency, oligopotency, multipotency, unipotency oligopotency, pleuripotency, unipotency, multipotency pleuripotency, multipotency, oligopotency, unipotency
- Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.Oligopeptide 1 Oligopeptide 2 N. N- H. N-H H Give the three-letter and one-letter names of the amino acids in each oligopeptide starting from the amino terminal to the carboxyl terminal. Make sure that the amino acid names are arranged in CORRECT order for both oligopeptides.
- Choose from A-F. This amino acid may serve as a phosphorylation site, and turn on or off the protein. H3N-C-H H3N-C-H CH2 H2N CH 2 H-C-OH CH2 H2C CH2 CH3 CH3 Choice "A" Choice "B" Choice "C" COO H,N-C-H H,N-C-H H3N-C-H CH2 CH2 C=CH C-NH CH2 NH | CH SH C-N Choice "E" Choice "F" Choice "D"tide c lirectir as ques ar to t synthr direct s, the secon aft 43. Peptide bond formation has a positive AG. What is ATP's role in making protein synthesis favorable?bob D Lipid Functional protein E 0=210 [Choose ] [Choose]
- c. When two nucleotides have hydrogen bonds between their bases (base paired), the sugar phosphate backbones are always choose one: (parallel / antiparallel) d. In RNA the purine base A (adenine) pairs with the pyrimidine base (guanine) pairs with the pyrimidine base choose one: (opposite / matched / complementary / dimerized ) and the purine base G This is referred to as being18 The image below shows the different interactions responsible for the spontaneous folding of a protein molecule. Identify which interactions are involved for each labelled region 0-H H CH,OH CH, NH, 0 B O-H--OO CH, CH₂ A B D C A यह मह CH CH₂COOH C H CH, CH, CH, CH H--O=C D T (CHJANH, - interactions ion-dipole interaction Hydrogen bonding Hydrophobic interactions Disulfide bonds lon-ion interaction 18Please ASAP. Thank you. Hyperpolarization activated cyclic nucleotide modulated channels (HCN). How is this channel activated? What is predominant ion that flows through this channel?