Question

In: Biology

please answer the following detailed in a paragraph. I am really struggling with this concept. thanks!...

please answer the following detailed in a paragraph. I am really struggling with this concept. thanks!

Microorganisms can thrive under many different conditions, including high-temperature environments such as hot springs. To function properly, cell membranes have to be in a fluid state. How do you expect the fatty acid content (saturated versus unsaturated) of bacteria living in high-temperature environments might compare with that of bacteria living in more moderate temperatures?

2. Heating a protein sufficiently may cause it to denature. Considering the definition of denaturation, what does this statement say about the strengths of peptide bonds in comparison to hydrogen bonds?

Solutions

Expert Solution

Answer:

1):

  • the microorganisms which live in extremely hot environments are called as hyperthermophile..
  • the cell membrane of these microorganisms contain high levels of saturated fatty acids to retain cell membrane shape/integrity, along with high permeability barriers for proper functioning of lipid membrane.

2):

  • As we know, the proteins are polymers of amino acids and have peptide bond between two amino acids.
  • for proper function and shape, a protein or an enzyme needs an ambient temperature.
  • if temperature increased, protein denatured, their secondary and tertiary structures altered but the peptide bond (between two amino acids ) of primary structure remain intact.
  • if a protein in (A) quaternary structure - denaturation - the protein sub-units are dissociated and spatial arrangement of of protein sub-units is altered/disrupted.
  • protein in (B) tertiary structure - denaturation - covalent interaction between amino acids side chains disturbed.
  • eg. disulfide bridges between cysteine groups, non-covalent dipole -dipole interactions between polar amino acids side chain and surrounding environment (solvent - water), van der waals interactions between non polar amino acids side chain.
  • protein in (C) secondary structure - denaturation - regular repeating pattern of alpha helics and beta-pleated sheets is lost.

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