Question

What will happen if some of the hydrogen bonding capable groups such as C=O, O-H or...

What will happen if some of the hydrogen bonding capable groups such as C=O, O-H or N-H do not form hydrogen bonds in the folded protein?

Homework Answers

Answer #1

There are number of interactions which are there to stabilize the folded structure of proteins. One of the most important one is H bonding .

When some of the hydrogen bonds are not there in the folded protein , it tends to destabilize the protein and favours the unfolding of the protein structure.

It plays an important role because it is H bonding which stabilize the secondary , tertiary and quatnary structure of protein and the core of most protein is composed of secondary structure ie alpha helix and beta sheets.

So basically it is the central feature for the stability of protein molecules.

Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
4. Why is an HCN•••HF hydrogen bond linear (N–H–F angle is 180o), while the hydrogen bonding...
4. Why is an HCN•••HF hydrogen bond linear (N–H–F angle is 180o), while the hydrogen bonding geometry in an H2CO•••HF interaction is trigonal planar, with an O–H–F angle of 120o?
1. For protein secondary structure, which of the following is incorrect? A. Secondary structure consists of...
1. For protein secondary structure, which of the following is incorrect? A. Secondary structure consists of α-helices and β-pleated sheets B. The interactions between C=O and N-H groups are hydrogen bonding interactions C. Secondary structure is created by bonding between C=O and N-H groups in the peptide backbone D. A protein can have either α-helices of β-pleated sheets, but never both 2. With regard to protein folding and denaturation, which one is incorrect? When egg white solidifies during heating, this...
This is about hydrogen bonding. 1. Can covalent bonds and hydrogen bonds be in the same...
This is about hydrogen bonding. 1. Can covalent bonds and hydrogen bonds be in the same molecule? 2. Do they(covalent bonds) have to be present for Hydrogen bonding to take place? 3. And if so are Covalent bonds stronger then the Hydrogen bond? Is this always the case? 4. And what is the significance of knowing that covalent bonds are stronger? (Does it tell us any properties, or ...idk)
1. Which of the following statements best describes the hydrogen bonding network between deoxyhemoglobin (2HHB) and...
1. Which of the following statements best describes the hydrogen bonding network between deoxyhemoglobin (2HHB) and the Fe-Heme ligand? a)There are no direct hydrogen bonds between the ligand and hemoglobin amino acids, however there are 2 bridged hydrogen bonds that connect the Fe-heme to the protein via atomic oxygen. b)There are 2 direct hydrogen bonds between the ligand and hemoglobin amino acids. c)There are no direct hydrogen bonds between the ligand and hemoglobin amino acids, however there are 2 bridged...
Part A Determine the number of bonding groups for CH2Cl2. n = SubmitMy AnswersGive Up Part...
Part A Determine the number of bonding groups for CH2Cl2. n = SubmitMy AnswersGive Up Part B Determine the number of lone pairs around the central atom for CH2Cl2. n = SubmitMy AnswersGive Up Part C Determine the number of bonding groups for SBr2. n = SubmitMy AnswersGive Up Part D Determine the number of lone pairs around the central atom for SBr2. n = SubmitMy AnswersGive Up Part E Determine the number of bonding groups for H2S. n =...
What type of intermolecular forces exist between triethylamine and diethylamine? A) hydrogen bonding only B) hydrogen...
What type of intermolecular forces exist between triethylamine and diethylamine? A) hydrogen bonding only B) hydrogen bonding and dipole-dipole forces C) hydrogen bonding, dipole-dipole forces, and dispersion forces. D) Dispersion forces only. Please give reasoning.
One way to destabilise a folded protein structure is to change the solution conditions so that...
One way to destabilise a folded protein structure is to change the solution conditions so that the backbone NH and CO groups in the polypeptide chain form stronger hydrogen bonds with other components of the solution (compared to the hydrogen bonds that they form with each other in the folded protein). Which of the following perturbations is most likely to destabilise a protein in this way? Select one: a. Adding a high concentration of guanidine b. Changing the pH of...
Here are some uncommon functional groups, predict and justify whether each is an o/p or a...
Here are some uncommon functional groups, predict and justify whether each is an o/p or a meta-director for electrophilic substitution when attached to a simple phenyl ring by the open bond: -O-CF3   -N=O    -O-SO2-OMe
O-H bond in a water molecule is about 20 times larger than that of the hydrogen...
O-H bond in a water molecule is about 20 times larger than that of the hydrogen bonds between water molecules in liquid water. Fractionally, how much lower is the evaporation rate of OH from liquid water as compared to water molecules? Please provide an estimate.
Indicate whether the following statements describe the primary, secondary, tertiary, or quaternary protein structure. (More than...
Indicate whether the following statements describe the primary, secondary, tertiary, or quaternary protein structure. (More than one can apply to the below) A) R groups interact to form disulfide bonds or ionic bonds. B) Peptide bonds join the amino acids in a polypeptide chain. C) Several polypeptide chains in a beta-pleated sheet are held together by hydrogen bonds between adjacent chains. D) Hydrogen bonding between amino acids in the same polypeptide gives a coiled shape to the protein.