Define hydropathy and how that can be used to determine protein structure.
Hydropathy plot is based upon the hydrophobicity or hydrophobic character of a series of amino acids present in a polypeptide sequence. This plot is helpful for determination of membrane spining domains, regions that are exposed towards exoplasmic side or lumen side. Based upon the hydrophobic and hydrophilic properties of 20 amino acids a hydropathy scale is present. The X axis of the graph represents the amino acids and Y axis represents the summed hydropathy at each point of sequence. By determination of hydrophobic region of a peptide sequence membrane spinning region or interior portion of a globular protein could be analysed.
Define hydropathy and how that can be used to determine protein structure.
1) a. Write two methods that can be used to determine protein primary structure b. what is the purpose of CNBr and betamercaptoethanol in determining protein primary structure?
9. Draw a hydropathy plot of a 330 amino acid long singlepass transmembrane protein that has a TM region beginning at residue 55. Generally, how long would you have to draw the TM region? 17. Describe two examples of membrane protein constraint and why it is important in each system. Draw diagrams.
Draw a hypothetical hydropathy plot of the connexin protein (approximately 350 aa). Use arrows to point to different parts of the plot to make 5 distinct features about it
1-3 thank you Define and describe protein 1 degree, 2 degree, 3 degree, 4 degree structure c know amino acid sidechain know forces that determine protein 30 structure Define protein and domain families
Describe fluorescence correlation spectroscopy and how it is used to study protein structure.
4. (a) Define the four levels of protein structure (primary, secondary, tertiary, and quaternary). (2 pt) (b) List four examples of types of interactions which give rise to tertiary structure. (2 pt) (c) What is protein denaturation, and list at least three ways this can be achieved. (2 pt)
1. How can protein folding affect protein function? 2. How can amino acid sequence affect protein function? 3. How can an amino acid sequence (primary sequence) dictate 3D protein structure?
pls try expaling this concept in as much detail as possible . this is all the informetion i eqs given to anserw the question myself Hydropathy plots are a measure of the hydrophobicity of a protein. The free energy for transferring an amino acid in a protein from the membrane to water is plotted as a function of the position of the helix in the sequence in the protein. Numbers greeter than +84 kJ/mol on a hydropathy plot are indicative...
Can you determine protein-protein interation from qPCR? If so, please explain how.
please answer me this Consider a membrane protein destined for the plasma membrane. From a hydropathy plot, you determine the protein has the following general structural elements: • • • 5 Trans-membrane domains (boxes 1-5) 6 soluble domains (wavy lines A-F) Flanking charges around trans-membrane domain 1. (A positive charge is towards the N-terminus, and a negative charge is towards the C-terminus.) You find that soluble domains B and E contain possible glycosylation sites. Ntorm in an ammo u arom...