MSA- multiple sequence alignment is the alignment of proteins in specific sequences according to their occurance in different forms like in secondary and tertiary structures. These sequences can also help in knowing the sequence of even nucleotides or amino acids. Yes, different types of them have certain patterns through which they are easily recognised. In case of Alpha helix in protein sequences, the secondary structure of proteins is twisted into a right handed manner with hydrogen bond formation between N-H group of one amino acid to the C=O group of another amino acid . The another amino acid is 4 residues away. The major difference in the beta sheet in MSA is that they are made up of pleated sheets of amino acids residues of beta strands that are linked together by hydrogen bonds. Both the structures in MSA have hydrogen bonding but they have different structure and bonding is between different amino acids. In Beta sheets ,the bonding is with the adjacent amino acid only. So we can easily recognise the difference despite between some common similarities.
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How do you know if an MSA is in an alpha helix or beta sheet?? Do...
Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group 1. d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
1. Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
How do you interpret the alpha and beta for the stock?
Question 1 (Mandatory) (1 point) The following is an example of_ H-N a parallel alpha-helix a parallel beta-sheet an antiparallel alpha-helix an antiparallel beta-sheet ● a domain
Understand alpha helices and beta pleated sheets Question How is it possible for the a-helix to have amino acids with bulky side chains while the B-pleated sheets cannot? Select the correct answer below: O The R groups in the a-helix stabilize the structure, while they interfere with the hydrogen bonds in a B-pleated sheet. The R groups are contained inside the a-helix structure, while they interfere with the hydrogen bonds in a B- pleated sheet. O The R groups lie...
ter 9. Hemoglobin and Myoglobin Which of these is not found in myoglobin? A) alpha helix b) beta sheetc) heme group, d) globular folding pattern • Which statement about hemoglobin is not true? A) it is globular b) it contains helix loop-helix c) it has three subunits d) it has heme groups · The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these - The...
Why will the phi/psi angles of an amino acid in an alpha-helix be different from the phi/psi angles of an amino acid in a beta-sheet? How are phi/psi angles possible fro Pro and for Gly different from those of other amino acids?
Sort each peptide chain as part of a parallel fi sheet, part of an antiparallel beta sheet, either (cannot determine if parallel or antiparallel), or not part of a fi sheet (for example, if it is part of an alpha helix). Be as specific as possible. For example, if a given structure is a parallel fi sheet, identify it as such.
How to find Moseley's parameters for K-alpha, K-beta, L-alpha, and L-beta X-Ray Fluorescence? Could you explain explicitly? If you find them online, please cite the webpage. Thank you!
Consider an important protein like beta-galactosidase, which breaks down lactose. Many bacterial species have beta-galactosidase. But that doesn't mean that the amino acid sequence of beta- galactosidase in all those bacterial species is exactly the same. Far from it. As bacteria diversified into different species over evolutionary time, beta-galactosidase encoded in the genomes of the bacteria also diversified. However, we can assume that even though beta-galactosidase diversified, it was under pressure to maintain structure and function, because the reaction it...