Why heating, changes in pH and other environmental changes can interfere with the function of proteins?

Question

Please let me know what other "environmental changes" or factors aside heat, chemicals and salt concentration that can interefere with protein functions. Thanks!

Answer 1

When a protein is heated, subjected to a significant pH changes, or treated with certain chemicals, its structure can become disordered and the coiled peptide chain can unfold to give a more random conformation. This unfolding, which is due to the disruption of hydrogen bonds and ionic bonds, is typically accompanied by a loss of normal function, which is also known as denaturation of protein. You remember the primary, secondary, tertiary, and quaternary structure of protein? The "environmental changes" greatly disrupts the 3D shape of tertiary and quaternary structure of protein. As far as other "environmental changes" besides the ones you've listed... I don't recall any from the books I've read. Probably because I'm a Chem major... and not Bio. =P I hope this helps though. Good luck on your Bio!

Answer 2

Proteins are complicated 3 dimensional structures made out of amino acids. the three dimensional structures are maintained by technique of the interactions of each and every of the amino acids in a protein. those interactions contain acidic and undemanding amino acids being attracted to at least one yet another, hydrogen bonding and van der Waals forces. at the same time as our surroundings of the protein adjustments, those forces between the amino acids contained in the proteins may also change. at the same time as the magnitudes of the forces change, the protein can change its structure in 3 dimensions even with if the string of amino acids does no longer change. therefore our surroundings is extreme contained in the three dimensional structure of a protein. the three dimensional structure is extreme for the right functioning of the protein. So, a protein in an surroundings of the incorrect pH does no longer artwork. some proteins, which contain the tummy digestive enzymes pepsin and gastricin want a pH that's totally acidic (contained in the variety of two-3) to catalyze the breakdown of injested proteins. At a intense pH, they don't artwork because they do no longer have the right 3 dimensional structure. notwithstanding, this pH might want to render different enzymes inactive because they want a extra alkaline surroundings with larger pH.

Answer 3

This may sound silly, but last year I couldn't remember the exact answer to your question on a lab exam. If I remember correctly, the other factor is "mechanical stress." I don't remember what exactly that means, but maybe now you can look it up...