Explain what is meant by "The Central Dogma"? In your explanation, describe the structure and function of the macromolecules that are important in this process. Describe at least two deviations to the Central Dogma.
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- Explain what is meant by “The Central Dogma”? In your explanation, describe the structure and function of the macromolecules that are important in this process. Describe at least 4 deviations to the Central Dogma.I was given an amino acid position 564 with the PDC code 2V1X. Would it be possible to describe why this position in the protein is important and outline the effects the mutation will have on the structure / function of the protein? Thank you.Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
- Indicate which of the following are present in the primary, secondary, tertiary, and quaternary structures ofproteins: a. peptidebonds b. hydrogen bonds between adjacentpeptides c. hydrogen bonds within a singlepeptide d. hydrophobic interactions e. association of four polypeptide chainsa) In the article the authors reference the canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do the authors suggest that other intermolecular interactions must be important to fully understand folding processes? https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6995338/pdf/nihms-1067149.pdfThe chain 3 subunit contains the amino acid sequence shown below. This sequence contains one alpha helix and the rest is random coil. Mark the region you believe will contain the alpha helix and explain your choice. In needed, feel free to use a helix wheel or other tools as part of your explanation. MNTFIIFIILIPIVGFALLAVNILLAVYKP D. Focus es) 9: J) ENG 83°F 6/19 DELL
- 1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein? 2) What are detergents and why are they useful? How do they basically work? 3) What is meant by amphipathic? What is an example of this?Rationalize the following observations.(a) Serine is the amino acid residue that can be replaced with theleast effect on protein structure and function.(b) Replacement of tryptophan causes the greatest effect on protein structure and function.(c) Replacements such as Lys -> Arg and Leu -> Ile usually havevery little effect on protein structure and function.1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)
- Using one of the lower level structures, explain how the protein’s effects one of the higher level of structure (primary influencing tertiary, secondary influencing tertiary, tertiary influences on quaternary, ect.)Which of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)? Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic.Mark as true or false the statements about amino acid reactivity and peptide synthesis: ( ) Peptides are very diverse in terms of their function/application. Some are hormones or their releasing factors, some are neurotransmitters, some are toxins, some are natural antibiotics, and some work as sweeteners, such as aspartame. ( ) Most of the natural peptides occur in low concentration, which makes their isolation from the matrix difficult, and therefore, their chemical synthesis is necessary. ( ) The chemical synthesis of peptides is only done with the use of enzymes ( ) A difficulty in the synthesis of peptides is due to the fact that carboxylic acids and primary or secondary amines do not form amide bonds easily. When mixing the two, what we would have would be products from the transfer of protons between them, forming a charged species. ( ) The chemical synthesis of peptides uses a chemical reagent to activate the carboxylic acid of the amino acid, which will undergo nucleophilic…