The mitochondria precursor protein is imported as an unfolded polypeptide chain. How are those polypeptide chains kept in an unfolded state following their synthesis in cytosol ?
mitochondrial protein are synthesized by ribosomes which are present freely in the cytosol. ribosome binds with the m RNA of mitochondrial protein and then synthesise it in the cytoplasm and then assemble it into a vescicle and then transport to the mitochondria. mitochondrial protein have mitochondrial targeting sequences as follow:
For matrix protein - Matrix targeting sequence
For inner and outer membrane transmembrane proteins- inner and outer membrane targeting sequence respectively.
due to these targeting sequence mitochondrial proteins are targeted to the particular section of Mitochondria and then get stabilized.
I am giving the complete idea about all this process into the diagrams and go through it.
The mitochondria precursor protein is imported as an unfolded polypeptide chain. How are those polypeptide chains...
How many polypeptide chains are shown in the quarternary structure of the protein ? What types of bonds and interactions hold the quaternary structure in place Mouetelh Structure (Part B) Tertiary Structure ーCH CH-SS CH CH NH -CH2 CH, CH CH Quaternary Structure CH CH Three polypeptide chains CH2 Protein Structure
The ER signal sequence on a growing polypeptide chain is recognized by a signal-recognition particle (SRP) in the cytosol. What does this interaction accomplish? It cleaves the ER signal sequence from the polypeptide chain. It cleaves the ER signal sequence from the polypeptide chain. It guides the ribosome and its polypeptide to the ER. It releases the polypeptide chain from the ribosome. It speeds the synthesis of the polypeptide chain. Which of the following choices reflects the appropriate order of...
35. Insulin is a polypeptide hormone that contains two short polypeptide chains linked by two interstrand disulfide bonds. In order to sequence the polypeptide chains, the most logical order of events to perform would be: I: Reduce the peptides with mercaptoethanol. II: Sequence the peptides using Edman degradation. III: Separate the peptides by gel filtration. IV: Alkylate the peptides with iodoacetate a) I, IV, III, I 36. Which ONE of the following statements regarding chaperonin is INCORRECT? The majority of...
1.Hemoglobin is a complex protein that contains four polypeptide chains. The normal hemoglobin found in adults –called adult hemoglobin –consists of two alpha and two beta polypeptide chains, which are encoded by different loci. Sickle-cell hemoglobin, which causes sickle-cell anemia, arises from a mutation in the beta chain of adult hemoglobin. Adult hemoglobin and sickle-cell hemoglobindiffer in a single amino acid: the sixth amino acid from one end in adult hemoglobin is glutamic acid, whereas sickle-cell hemoglobin has valine at...
If a protein is composed of the two polypeptide chains connected together via two disulfide bonds with no free sulfhydryl groups. The protein was treated with mercaptoethanol to break its disulfide bonds, and then the mercaptoethanol was removed so that disulfide bonds could re-form. How many different arrangements of disulfide bonds are possible? (the protein has a total of 4 Cys and 2-bonds) Please, explain your answer in detail.
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein - that is, its overall shape and how the chains are "folded” around each other - is very important for its function. In an aqueous environment, in an active, folded state the hydrophilic amino acids in the protein are facing outwards exposed to the water and the hydrophobic amino acids are hidden away from the water in the core of the protein. In a...
1. Where is the ER targeting sequence located in the polypeptide chain (N-terminal, interior, or C-terminal) 2. Name 4 organelles that require organelle specific targeting sequences in polypeptide 3. Name 3 final locations for proteins with ER signal sequence 4. Satranslational translocation: (a) Name the protein that the signal sequence binds to (b) Name the protein SRP binds to 5. State the function of signal peptidase 6. Name a membrane protein that is not a single pass membrane protein 7....
Question 2 How is a protein targeted to the matrix of mitochondria in a eukaryotic cell? Describe the “travels” of a newly transcribed polypeptide as it goes from ribosome to its destination in the matrix. (Hint: the words “contact site” should occur somewhere in this description if your polypeptide is traveling the right path.)
How would I determine the equilibrium ratio of folded to unfolded molecules of protein at a certain temperature (25 C) and standard state free energy (-11.4 kJ/mol)?
Which of the following statements are true about protein domains? I. Polypeptide chains longer than 200 amino acids in length have multiple domains. II. Domains are tertiary structural components of proteins. III. Different domains are encoded by different exons of a gene. IV. Each domain in a protein has a specific function. A. I, II, III, and IV B. I, II, and III C. II, III, and IV D. II and IV E. I and IV