| Book Edition | 8th Edition |
| Author(s) | DeCoste, Zumdahl |
| ISBN | 9781305581982 |
| Publisher | Cengage Learning |
| Subject | Chemistry |
What if you contracted a disease that prevents all hydrogen bonding in proteins? Could you live with such a condition?
bio.libretexts.org/Bookshelves/Biochemistry/Book%3A_Biochemistry_Free_and_Easy_(Ahern_and_Rajagopal)
ncbi.nlm.nih.gov/books/NBK470235/
-If you contracted a disease that prevents all hydrogen bonding in proteins then you can not live with such a condition.
-This is because hydrogen bonding is involved in the secondary, tertiary, and quaternary structure of protein which makes a protein functional.
-The polypeptide backbone forms a repeating helical structure that is stabilized by hydrogen bonds between a carbonyl oxygen and an amine hydrogen.
-These hydrogen bonds occur at regular intervals of one hydrogen bond every fourth amino acid and cause the polypeptide backbone to form a helix.
-In the β-pleated sheet, the "pleats" are formed by hydrogen bonding between atoms on the backbone of the polypeptide chain.
-Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.
-The correct three-dimensional structure is essential to function.
-Folding is a spontaneous process that is mainly guided by hydrogen bonding.
