Which of the following statements is not true about protein folding ? *Protein folding is a process by which a polypeptide chain form a stable 3D structure.Protein folding leads to loss of function and causes a wide range of diseasesWhen protein is defolded, peptide bonds are not affected.Protein folding is essential for proper function of proteins.

The folding of Protein is an important cellular process that occurs in the Endoplasmic reticulum.…

Answered: Which of the following statements is…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 2VCQ: Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble...

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Similar questions

Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble protein, and which would you expect to find in the interior? What distribution of amino acids would you expect to find in a protein embedded in a lipid bilayer?
Describe the four levels of protein structure. How do a proteins side groups influence its interactions with other substances? What happens when a protein is denatured?
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
Which of the following statements concerning complete protein hydrolysis is incorrect? Primary structures are preserved Tertiary and secondary structures are disrupted All peptide bonds are broken Water is a reactant in the process
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acids
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.
Which levels of protein structure are determined by primary structure (i.e. the specific amino acid sequence beginning at the amino terminus of the polypeptide)? Mark all that apply. 1. secondary structure (alpha helices and/or beta sheets) 2. tertiary structure (the folded, three-dimensional shape of a protein) 3. amino acids 4. peptide bonds
Which levels of protein structure are determined by primary structure mark all that apply 1. secondary structure (alpha helices and/or beta sheets) 2. tertiary structure (the folded, three-dimensional shape of a protein) 3. amino acids 4. peptide bonds
Which of the following is an example of secondary protein structure?A) DipeptideB) TriglycerideC)α -helixD) Amino acidE) Fatty acid
Which statement about quaternary structure is TRUE? Quaternary structure is unaffected by acids or heat. Quaternary structure is determined by the same interaction that holds an α-helix together. Quaternary structure is how prosthetic groups are held in a protein. Quaternary structure is the position of subunits in the overall structure of a protein. All proteins have quaternary structure
Which type of protein is classified by a polypeptide which is arranged in long strands or sheets? fibrous proteins globular proteins membrane proteins intrinsically disordered proteins

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