|
Denaturation (biochemistry) - Wikipedia, the free encyclopedia
|
||
|
The function of a protein (except when it is serving as food) is absolutely dependent on its three-dimensional structure. A number of agents can disrupt this structure thus denaturing the protein. ... As mentioned above, high temperatures can denature proteins, and when a cell is exposed to high temperatures,
|
||
|
Anything that destroys H-bonds, ionic bonds, or hydrophobic interactions will denature a protein ... Disulfide bonds can be broken with reducing agents...
|
||
|
Clues as to what stabilizes the tertiary structure of a native protein can be gained by subjecting proteins to agents that unfold or denature a protein. Such agents include extremes of pH, high concentrations of some salt solutions or organic solvents, and temperature extremes.
|
||
|
A manufacturing process to prepare two antiretroviral agents that denature the HIV-1 nucleocapsid protein (NCp7) has been developed and demonstrated on a pilot scale. ... Phillip J. Fiore, Timothy P. ... Chemical Development Department, Parke-Davis Pharmaceutical Research Division, 188 Howard Avenue, Holland, Michigan 49424...
|
||
|
Types of Microbial Control Agents ... Protein function depends on the 3-D shape of the molecule. Extreme heat, or certain chemicals, can denature, or change the shape of a protein. A denatured protein can no longer carry out its function within the cell.
|
||
|
Bubbles and foaming are caused by proteins in aqueous solution forming films at the air/water interface. Foaming must be avoided because protein can denature at the surfaces formed by these interfaces. Many antifoaming agents are on the market;
|
Copyright © 2009, Dictionary.com, LLC. All rights reserved.