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- 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.Which model (2D topology or trRosetta) is likely a better representation of the actual protein AlaE, why?The temperature of unfolding (denaturation) for a particular protein is 50 oC. A replacement of several amino acids within the protein increased the enthalpy of protein unfolding from 7 kJ mol-1 to 9 kJ mol-1 and did not affect the entropy of unfolding.Calculate the temperature of unfolding after the replacement.
- The number of distinct protein folds in limited. Why might this be so?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."No plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.
- The Energetic Cost of Peptide Elongation How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?You have isolated a new protein called STICKY. You can predict from comparisons with other known proteins that STICKY contains a bHLH domain. Predict the function of STICKY and rationale forthe importance of these domains in STICKY function.Answer for each 1, 2, 3, 4 and 5 labelled in the attached image: a)What is this molecule? b)What superfamily does it belong to? c)Which number points to the peptide binding domain? Thank you!
- Loop regions play important roles in the secondary structure of protein. Define loop region and give three (3) of the rolesTrue or False: 1.Functional proteins also undergo chemical modifications like the removal of the first amino acid cysteine. 2.Operational messenger RNA transcripts travel to the cytoplasm for translation after intron removal, capping the 3’end and poly -A tailing the 5’end.Both hsp60-like and hsp70 molecular chaperonesshare an affinity for exposed hydrophobic patches on pro-teins, using them as indicators of incomplete folding. Whydo you suppose hydrophobic patches serve as critical sig-nals for the folding status of a protein?