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What does enzymes functions depend on?
The function of an enzyme is dependent on the shape of the enzyme. The structure and shape determines what the enzyme can do.
Why does the structure of a protein or enzyme determine its function?
Yes.
What happens to an enzyme and structure as it exceeds the typical human body temperature?
The enzyme can denature and will not function because it is no longer in the proper shape.
What determines the enzyme's function?
Its composition and physical structure - this is determined by the DNA/RNA that coded for it.
What is the key feature of a protein or enzyme that makes its function correctly?
The most important feature that makes functional to a protein or an enzyme is its three dimensional structure based on its tertiary structure. Either, a structural protein, where alpha helices and beta sheets are vital to its function, or an enzyme, where the shape of its active site is crucial for its biological activity, the tertiary structure is the most important characteristic. In fact, the process called "protein folding" is one of the key biochemical areas of study for the scientific community.
What does enzymes functions depend on?
The function of an enzyme is dependent on the shape of the enzyme. The structure and shape determines what the enzyme can do.
Why does the structure of a protein or enzyme determine its function?
Yes.
Is renin a hormone?
by function is enzyme ... by structure is hormone
How structures affects function?
The structure is important because each enzyme's shapes allows only certain reactants to bind the enzyme.
What happens to an enzyme and structure as it exceeds the typical human body temperature?
The enzyme can denature and will not function because it is no longer in the proper shape.
What determines the enzyme's function?
Its composition and physical structure - this is determined by the DNA/RNA that coded for it.
What is lost when an enzyme is denatured?
The enzymatic function of the enzyme is lost when it is denatured. Of course this also means that the enzyme's structure has changed too. Depending on the severity of the denaturation, the enzyme may be able to revert back to its original structure once the abused conditions are removed.
A noncompetitive inhibitor has a structure that?
A noncompetitive inhibitor has a structure that does not resemble the substrate structure. A compound that binds to the surface of an enzyme, and changes its shape so that a substrate cannot enter the active site is called a noncompetitive inhibitor.
Give an example of the relationship between structure and function?
One example of the relationship between structure and function is found in enzymes as their function is dependent upon its structure. Enzymes are catalytic proteins that speed up a reaction without being consumed. Their protein structure enables them to recognize their substrates, even among isomers, thus allowing them to catalyze very specific reactions. The interactions between a protein's primary structure, its amino acid sequence, determine its secondary structure of hydrogen bonded alpha and beta pleated sheets. The side chains of the amino acids help determine the next superimposed structure, the tertiary structure and the quaternary structure if the protein has one. A protein's conformation enables it to form an active site whose shape is compatible with that of the substrate. Once the substrate enters the active site, the enzyme's structure is altered as induced fit moves the active site's chemical groups into positions that enhance their ability to catalyze the chemical reaction, thus improving the enzyme's function. An enzyme's structure is so closely correlated to its function that even a slight change in a protein's primary structure can affect its conformation and ability to function. For example, although noncompetitive inhibitors bind to the enzyme away from its active site, they alter the enzyme's conformation so that the active site no longer has the right structure to bind with the substrates, preventing it from functioning correctly.
Do antibodies have a quaternary structure?
No. It is possible for an enzyme to have a quaternary structure, but it strictly depends on the enzyme. For example, β-galactosidase, more commonly known as lactase, is the enzyme that breaks the β linkage between the disaccharide lactose into its componenets glucose and galactose. β-galactosidase is a tetramer, meaning it has four subunits. This is an example of an enzyme with a quaternary structure. Enzymes can also be tertiary structures, meaning only one subunit. The quaternary structure is just made up of more than one tertiary structures. Depending on the enzyme, it can either function with only one amino acid chain coiled into a conformation (tertiary) or a group of amino acid chains coiled into a conformation (quaternary).
What is the key feature of a protein or enzyme that makes its function correctly?
The most important feature that makes functional to a protein or an enzyme is its three dimensional structure based on its tertiary structure. Either, a structural protein, where alpha helices and beta sheets are vital to its function, or an enzyme, where the shape of its active site is crucial for its biological activity, the tertiary structure is the most important characteristic. In fact, the process called "protein folding" is one of the key biochemical areas of study for the scientific community.
What effects does acid have on ezyme?
Acids can denature enzymes and make them less active or completely inactive. Denaturation causes a change in the three-dimensional structure of an enzyme which can affect the function of the enzyme.
