Off the top of my head: techniques such as chemical and enzymatic degredation (particularly if they are targeted) coupled with various analytical techniques particularly mass spectrometry and NMR. X-ray crystallography could also be used if the enzyme can be crystallised.
Usually with X-ray crystallography since it is very accurate but it is often also very hard to crystallize proteins, them being macromolecules with complex structures. X-ray crystallography also cannot obtain the structure of the protein in vivo since the crystal structure of a protein may be different from its structure in vivo. NMR (nuclear magnetic resonance) can be used to determine the in vivo structure of proteins but the resolution is usually lower.
An enzyme is a protein and the primary structure of a protein is the unique sequence of amino acids making up a polypeptide chain which, ultimately, will determine the structure/function of the protein.
Changes in pH or temperature decrease enzyme activity because bonds b reak and the enzyme returns to it's PRIMARY structure. (not tertiary)
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).
An enzyme
prevent the substrate from binding the enzyme's active site
active site
Yes.
Quaternary and Tertiary levels of protein structure principally determine the active site of an enzyme.
no
Primary structure
There are several things that determine an enzyme's activity. The main determinants include the structure of the enzyme, temperature, pH and so much more.
Changes in pH or temperature decrease enzyme activity because bonds b reak and the enzyme returns to it's PRIMARY structure. (not tertiary)
DNA is the molecule most responsible for determine traits such as eye color, body structure, and cellular enzyme production.
The function of an enzyme is dependent on the shape of the enzyme. The structure and shape determines what the enzyme can do.
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.
The most common methods used for the determination of protein structure are X-ray crystallography or NMR spectroscopy.
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.
Primary