What makes the protein folding process mysterious? X: There appears to be no intermediate states of stability. Y: There is no way to visualize the complete folding path. Z: Proteins tend to be "native" or "denatured." X and Y Y and Z X and Z O X, Y and Z O X only

What makes the protein folding process mysterious? X: There appears to be no intermediate states of stability. Y: There is no way to visualize the complete folding path. Z: Proteins tend to be "native" or "denatured." X and Y Y and Z X and Z O X, Y and Z O X only

Name: What makes the protein folding process mysterious?X: There appears to
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Description: What makes the protein folding process mysterious?X: There appears to be no intermediate states ofstability.Y: There is no way to visualize the complete foldingpath.Z: Proteins tend to be "native" or "denatured."X and YY and ZX and ZX, Y and ZO X on

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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Protein folding a. is essential to make a functional protein and occurs spontaneously b. is mediated by peptide bonds and hydrogen bonnds c. is a random process essential for the 3D shape of the protein d. is essential to make a functional protein and occurs with the help of chaperones
Which of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.
During the folding of a protein in a buffered aqueous solution, what happens to the entropy of the protein and the entropy of the water? The entropy of the protein decreases while the entropy of the water increases. Both the entropy of the protein and the entropy of the water increase. Both the entropy of the protein and the entropy of the water decrease. The entropy of the protein decreases while the entropy of the water remains constant.
Which of the following, if any, is correct about protein folding? a)2° structure formation is primarily entropic, 3° structure formation is primarily entropic b)2° structure formation is primarily entropic, 3° structure formation is primarily enthalpic c)2° structure formation is primarily enthalpic, 3° structure formation is primarily entropic d)2° structure formation is primarily enthalpic, 3° structure formation is primarily enthalpic e)None of the above
What is the primary driver of protein folding on a macro level? a. Hydrogen bonding b. Van der Waals forces c. Covalent bonding d. Entropic force
Which of the following statements about chaperones is FALSE? a. Chaperones prevent incorrect interaction (i.e. aggregation) within and between non-native polypeptides thereby increasing the yield b. Chaperones are proteins c. Chaperones can greatly increase the rate of protein folding, and therefore, chaperones are enzymes. d. Chaperones do not specify correct folding e. Chaperones prevent aggregation of unfolded proteins
is this protein folding funnel from a metamorphic protein? yes or no? is there one intermediate that all pathways go through? yes or no?
A. What type of bond is ( the two mark wtih questions mark) B. What special amino acid side chain is involved in forming these bond C. Does this bond form unde reduction or oxidizing D. Is this bond seen more in cytoplsmic proteins or in extravellular protein
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? A mutation in the genetic sequence, which ultimately causes an amino acid to change(e.g. Trp – Asn – His turns into Trp – Arg – His) Dissolving a protein in a non-polar solvent (like oil) instead of water.
Can a mutation affect a protein's primary structure? Why or why not? Group of answer choices yes, a mutation could change a codon, which could change an amino acid yes, a mutation could change a fatty acid, which could change a glyceride no, a mutation will only affect DNA no, a mutation can affect protein secondary structure but not primary
Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structure
Non covalent bonds are very important in cell biology, could you explain why and provide an example that illustrates their importance ( do not chose protein folding as an example) What are the different levels of protein structure and what are the different parameters (sequence, type of bonds, etc...) that influence protein folding at these different levels?