How can you explain to a non-science person what is protein folding and how the concept is related to metabolic disorder. Explain in 2 paragraphs.
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How can you explain to a non-science person what is protein folding and how the concept is related to
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- Which of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..A particular DNA sequence encodes for MRNA that then encodes for the amino acid glutamate in a protein. A mutation occurs in the DNA that changes the MRNA codon for the glutamate into a different codon. Which change would cause the least disruption to the structure of the protein? Hint: Think about the nature of the various R groups (side-chains) of the amino acids, and how intermolecular forces/interactions govern the way a protein folds into its three-dimensional structure. The codon for the glutamate is changed into a stop codon. The codon for the glutamate is changed into the codon for aspartate. O The codon for the glutamate is changed into the codon for phenylalanine. O The codon for the glutamate is changed into the codon for serine.please describe the difference in these two macromolecule roles in cellular systems thank you
- The link between gene and protein was first articulated by Beadle & Tatum, who proposed the one-gene, one-enzyme hypothesis - which of the following statements contradicts this hypothesis? Sickle-cell anemia results in defective hemoglobin. Two enzymes are able to metabolize the same reaction. Alkaptonuria results when individuals lack a single enzyme involved in the catalysis of homogentisic acid. A mutation in a single gene can result in a defective protein. A single antibody gene can code for different related proteins, depending on the splicing that takes place post-transcriptionally.2a. The DNA is mutated on the 4th base pair to the following: DNA:3'TAC GAT GAG GTC TGA ACT 5 5' ATG CTA CTC CAG ACT TGA 3 2b. Does this mutation change the amino acid sequence? (Yes or No) If yes – what is new amino acid sequence? Protein:Could you please write a brief explanation about "Protein Evolution - Primary Structures of Proteins Reveal Evolutionary Relationships" please?
- The study of protein synthesis often uses a cell-free system where cells are ground with an abrasive to release the cell contents and then filtered to remove the abrasive. These mate- rials are added to the system, generating the indicated results: Materials Added Results Radioactive amino acids Radioactive protein produced Radioactive amino acids No radioactive protein produced and RNase (an RNA- digesting enzyme) What is the best interpretation of these observations?These multiple-choice questions are all related to the Basic Biological Principles (DNA) | Introduction to Biomolecules. Choose the best answer on the given choices.Let’s suppose we have downloaded the structure of Hemoglobin from PDB. Now we want to retrieve the location of helices and loops in it. How can we do it? How can we depict a protein’s coordinate info in a modeling program? (Subject: Bioinformatics)
- Choose the option that is best described by each of the following statements 1 1. Attacks the N-terminus 2. Uses proteins as substrates 3. Trypsin is an example 4. Breaks down short peptides 5. Cleaves C-terminal amide bonds 6. Pepsin is an example Aminopeptidase Protease aspartvl protease Peptidase Peptidase serine proteaseWhich of the following statements are correct about protein folding (select all that appy)? A. Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation B. The mature two-chain form of insulin spontaneously folds into the native conformation C. A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates D. Proteins randomly sample each possible conformation before arriving final native state E. Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red.