3. The important function of molecular chaperones to __________. A. move proteins from endoplasmic reticulum to the Golgi apparatus B. fold proteins into a native conformation C. add cofactors, coenzymes or prosthetic groups to proteins as they are synthesized D. assemble protein subunits into a quaternary structure E. transport proteins to either the plasma membrane or release them from cells to the extracellular space 4. Protein folding to a native conformation is highly dependent upon all of the following, except: A. the rotation about the peptide bond. D. the polar character of sequences of amino acids. B. The relative size of amino acid R-groups E. the rotation about the C?–N bond. C. rotation about the C?–C bond in the backbone.
Added by William C.
Close
Step 1
Step 1: The important function of molecular chaperones is to assist proteins in folding into their native conformation. Show more…
Show all steps
Your feedback will help us improve your experience
Dominador Tan and 58 other Biology educators are ready to help you.
Ask a new question
Labs
Want to see this concept in action?
Explore this concept interactively to see how it behaves as you change inputs.
Key Concepts
Recommended Videos
Proper folding of proteins is essential for their biological activity. In genetal, the functional conformation of a protein is the conformation with lowest energy. This means that if an unfolded protein is allowed to reach equilibrium, it should assemble automatically into its native, functioning folded state. Why then is there a need for molecular chaperones and chaperonins in cells? What different roles do molecular chaperones and chaperonins play in the folding of proteins?
2. Proper folding of proteins is essential for their biological activity. In genetal, the functional conformation of a protein is the conformation with lowest energy. This means that if an unfolded protein is allowed to reach equilibrium, it should assemble automatically into its native, functioning folded state. Why then is there a need for molecular chaperones and chaperonins in cells? What different roles do molecular chaperones and chaperonins play in the folding of proteins?Which enzyme better stabilizes the transition state? Which enzyme functions as a better catalyst?
Which of the following statements are correct? Explain your answers. A. Ribosomes are cytoplasmic structures that, during protein synthesis, become linked by an mRNA molecule to form polyribosomes. B. The amino acid sequence Leu-His-Arg-Leu-Asp-Ala-GInSer-Lys-Leu-Ser-Ser is a signal sequence that directs proteins to the ER. C. All transport vesicles in the cell must have a v-SNARE protein in their membrane. D. Transport vesicles deliver proteins and lipids to the cell surface. E. If the delivery of prospective lysosomal proteins from the trans Golgi network to the late endosomes were blocked, Iysosomal proteins would be secreted by the constitutive secretion pathways shown in Figure $15-30$ F. Lysosomes digest only substances that have been taken up by cells by endocytosis. G. N-linked sugar chains are found on glycoproteins that face the cell surface, as well as on glycoproteins that face the lumen of the ER, trans Golgi network, and mitochondria. H. Ribosomes bound to the outer nuclear membrane make proteins that are translocated co-translationally into the membrane.
Recommended Textbooks
Biology for AP Courses
Objective Biology for NEET
Introduction to General, Organic and Biochemistry
Transcript
18,000,000+
Students on Numerade
Trusted by students at 8,000+ universities
Watch the video solution with this free unlock.
EMAIL
PASSWORD
