It depends on the protein and how it was denatured - but no, not impossible. Sometimes it can be reversible, but it's usually only reversed in a test tube. Things become complicated in the actual biological system.
an antibody binding site.
Denaturation of a protein means loss of the protein's function due to structural change in the protein caused by some chemical or physical factor such as high temperature or unfavorable ph. The bonds that hold the structure together get affected which leads to the loss of structure and function
Denatured refers to when a protein loses its structure to become something akin to an amorphous blob. To really understand this though you must understand the structures of protein. A protein is a long string or chain composed of amino acids all linked together. When proteins are formed by the body they must 'fold' themselves into a structure that is capable of work or doing a task. Once in this folded form the protein can go on to serve whatever function it serves. Denaturing causes the protein to lose this shape and ultimately functionality. For the most part denatured proteins can be 'renatured' by reversing the cause of denaturing. A familiar example of denaturing while is non reversible is cooking eggs. The egg white is rich in proteins and when heated causes the protein to lose it's form and harden. As stated this can't be reversed.
Yes, enzymes are proteins and it is their sequence of amino acids (primary structure) that determines what kind of an enzyme it is and makes all the enzymes unique and it is the tertiary structure of enzymes that maintains their shape and give rise to the unique active site. When an enzyme is denatured, it loses its tertiary structure and therefore its shape.
Denatured refers to the loss of the 'native' active SHAPE of the enzyme - the Active Site included; this also causes the enzymes to lose their functions.
The shape of a protein allows it to perform its particular job.
Denatured proteins do not have any particular shape. A denatured protein is one that has broken amino acid interactions in the secondary and tertiary structures.
If a proteins shape is changed it has likely been denatured. This is often a breakdown and rearrangement of the protein.
The function of each protein is a consequence of its specific shape, which is lost when a protein denatures.
A protein is denatured because of high temperatures or changes in pH. When it is denatured, it means that the protein has lost its original shape and therefore, it cannot function properly anymore.
When a protein is denatured, its molecular shape is altered. This alteration may or may not be reversible.What remains is the primary structure of the chain(s) of the protein, in other words the sequence of the amino acids.The tertiary structure referers to the overall three dimensional shape will be lost
A protein is "denatured" when it inflates or deflates due to pH level, heat, Ect. Not sure if that's what you meant by losing its shape, though
Denatured protein. See attached Wikipedia Denatured Protein link. Denaturation. Proteins are fragile and its function depends on its 3D shape. High heat, salt concentration, pH, radiation etc will cause a protein to 'unravel' or change shape which leaves the protein nonfunctional. It is usually irreversible. Think of it as frying an egg. Eggs are protein right? When you fry an egg you change its shape and it is no longer opaque. You cannot unfry an egg.
There are two significant features of a denatured enzyme: 1) the enzyme does not have biological activity, either by the irreversible binding of an inhibitor or 2) the missing of it's tertiary structure, losing the proper "shape" for its biological functionality.
It has lost its active 3D structure and therefore it is not functional anymore.
Protein molecules change shape when you heat them. Then energy from cooking breaks some of the chemical bonds in the protein and this allows the molecule to take a different shape. This gives the food a more edible texture. The change is irreversible. It is called denaturing.
a denature protein may re-form to its functional shape when returned to its normal environment. what does that indicate about a protein's conformation? Proteins fold in natural environment (water) in a way that they are stable, but a non-polar solvent provides a very different environment, so the protein has to unfold and adopt a very different shape.
When a protein is denatured it involves the disruption and possible destruction of both tertiary and secondary structures. The denature of proteins can happen through the exposure of chemicals or heat.