Name the four different types of interactions responsible for creating tertiary structures in proteins
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- INSTRUCTIONS — Answer the Question properly and accordingly — Do not copy in Google, or here in Bartleby QUESTION • In general, proteins can be classified into 3 different groups. Name and give a short description of each type and how they are distinct from one another. Provide an example of a macromolecule or other complex structure representing each of the three types.INSTRUCTIONS — Answer the Question properly and accordingly — Do not copy in Google, or here in Bartleby QUESTION • In a globular protein, where would you expect the nonpolar regions to be located? Whereabouts would you expect the more polar regions to be found?Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
- Explain what the meaning of these distances is (e.g., from where to where?)Crystal structure of human monocyte chemotactic protein-2Here is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylatedGABA (B) Need help answering these questions about the GABA(B) protein. What class (globular, fibrous, membrane) protein is the protein Identify the organism (or organisms that have this protein) Identify the cellular location of this protein Describe the function Find the primary structure (list it on a slide) Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein) Find a picture of the tertiary structure (which should also show secondary structure) Does the protein have a quaternary structure, if so what is it?
- Can I get a flow diragram of the Central Dogma with the functions of the macromolecules which are important in the process and 4 deviations to the Central Dogma.Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?based on this oligopeptide (KEQSCMV) would someone be able to help me on the following questions? What moieties within oligopeptide are those mainly responsible for the formation of an alpha-helix? Name the process that leads to the unfolding of the alpha helix to yield a random coil. State and justify, for oligopeptide, which amino acid side chains will be involved in: hydrophilic interactions, hydrophobic interactions, disulphide bridges and salt bridges. In each case, briefly justify your choice.
- Exploring the nuanced landscape of protein dynamics, could you elaborate on noteworthy post-translational modifications (PTMs)? I'm interested in understanding specific examples of PTMs and gaining insights into their functional mechanisms. This inquiry delves into the intricate aspects of protein modulation within a biological context."The vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. Structures produced by X-ray diffraction are as good as the solutions from which they are derived they are false and I know that but explain why they are falseHydrophobic intercation associated with protein tertiary structure involve
