Explain how both alpha helices and beta sheets can be used by proteins that cross membranes. Also explain what a hydropathy plot is and how such a plot can be used to differentiate transmembrane alpha helices from transmembrane beta sheets.
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Explain how both alpha helices and beta sheets can be used by proteins that cross membranes.
Also explain what a hydropathy plot is and how such a plot can be used to differentiate transmembrane alpha helices from transmembrane beta sheets.
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- Describe the general structure of a type 2 alpha helix protein. Explain how type 2 alpha helix transmembrane domains can be used to form pathways for large polar and charged molecules to traverse the lipid bilayer of the cell membrane.explain how a hydropathy plot can distinguish proteins with single transmembrane domains from those with multiple transmembrane domainsCreate a ROUGH SKETCH (no need for exact hydropathy indices and residue numbers) of the hydropathy plot for the given membrane protein. -coo Please follow the color assignment of the helical domains and properly label the plot and axes. Here is an example: Amino Outside terminus Transmembrane helices are predicted by hydrophobic stretches of 20-25 aa residues 10 50 100 150 200 250 Hydrophobic Inside Hydrophilic Carboxyl terminus -3 10 50 100 150 200 250 Residue number Bacteriorhodopsin Hydropathy index
- The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in the solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface do. Determination of these rates can be used to explore the proteinfolding reaction, probe the tertiary structure of proteins, and identify the regions of protein–protein interfaces. These exchange reactions can be followed by studying the behavior of the protein in solvent that has been labeled with deuterium ( ²H), a stable isotope of hydrogen. What two methods described in this chapter could be readily applied to the study of hydrogen– deuterium exchange rates in proteins?Given the description of four different proteins above: Which protein will have the highest mobility in an SDS-PAGE gel?Roughly sketch the hydropathy plot for the given hypothetical membrane protein. Follow the color assignment of the helical domains and properly label your plot and axes (NB: Only a rough sketch is being asked. No need be exact with the hydropathy indices and residue numbers). CO-
- Make a table with a scale of absorbance and the concentration of protein in Chromatin sample from the following data for excel graph Absorbance=660nm following data are of tubes with concern A =0 B=0.036 C=0.011 D=0.001 E=0.027 F=0.020 G=0.032 H1=0.176 H2=0.183 I1=0.150 I2=0.171 also plot the graph??Draw a hydropathy plot and a 2D protein cartoon for a protein that passes through the lipid bilayer 6 times..Membrane-spanning proteins are notoriously difficult to characterize by x-ray crystallography. Hollonut of VISA Toplon a. Explain how the information in the diagrams below can be used in the detection of membrane- spanning proteins consisting of alpha helices, given that the lipid portion of a typical bilayer is approximately 30 Å thick. Amino terminus 5.4 A (3.6 residues) b. Identify and briefly describe how the features of a transmembrane protein composed of ß-sheets differ from that above.
- Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer.a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues thatcan be in each α-helixes for them to be long enough to span the bilayer?In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe- Ser-Gin-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys The hydrophobic residues in this sequence are presented in boldface type. Use helix wheel to demonstrate this peptide is an amphipathic helix.a) In the article the authors reference the canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do the authors suggest that other intermolecular interactions must be important to fully understand folding processes? https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6995338/pdf/nihms-1067149.pdf