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Why is a b-barrel as opposed to a b-sheet optimal for a transmembrane protein? Think about the energetics specifically.
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- For transmembrane proteins, either single-pass or multi-pass, the membrane spanning part of the protein usually assumes which of the following motifs? βαβ αβα α-helix β-pleated sheetExplain 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.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.
- An American biochemist Erwin Chargaff discovered that in the cells of all organisms he studied, the amount of adenine is always equal to the amount of thymine, and the amount of cytosine is always equal to the amount of guanine. Explain his findings.In cells, microtubule assembly depends on other proteins as well as tubulin concentration and temperature. What types of proteins influence microtubule assembly in vivo, and how does each type affect assembly?Given the description of four different proteins above: Which protein will have the highest mobility in an SDS-PAGE gel?
- Please describe the protein purification process with the aim of purifying a protein which locates on nucleus membrane.Transport of histidine into a bacterial cell was measured at several different histidine concentrations, see table below. Based on these data, is histidine uptake facilitated by a carrier or channel protein? a b Histidine (uM) 2.5 7 16 31 72 с Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. A carrier protein because it becomes saturated. A carrier protein because it does not become saturated. A channel protein because it becomes saturated. Transport (uM/min) d A channel protein because it does not become saturated. 42.5 119 240 490 1000 X Your answerWhich of the following statements are true? Electrostatic interactions are the dominant forces in protein molecular recognition. When two proteins form a complex there is an unfavorable loss of rotational-translational entropy. Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. Burial of an uncompensated positive charge inside proteins is usually unfavorable. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.
- What is Protein folding? Give at least 3 diseases that results from protein misfolding. Explain each. Can you give me a brief explanation about this question? Not less than 3 sentences.Maintaining nuclear RanGTP levels is critical for nucleo-cytoplasmic transport. Describe how mutations that disrupt RanGEF function would affect the movement of proteins coming in and going out of the nucleus.What effect will phosphorylation have on the behaviour of a protein on a 2D gel? 1. The spot corresponding to phosphorylated protein will be in the same position as that of unphosphorylated one. 2. Phosphorylated protein will run slower in the second dimension (SDS PAGE). 3. Compared to the spot of unphosphorylated protein, the spot corresponding to phosphorylated protein will focus during separation in the first dimension in an area with lower pH. 4. There will be shifts during both separation stages. O 3 O 1 O 4 O 2