The R groups of the amino acids in its active site
Shape of an enzyme specifically shape of its active site determines enzyme specificity .
Yes.
ATP synthase is the protein enzyme involved in chemiosmosis. It is responsible for generating ATP by facilitating the movement of protons across the inner mitochondrial membrane.
True. Protein is an essential building material for cells. It is involved in many cellular processes, such as structure, signaling, and enzyme activity.
The primary and secondary levels of protein structure determine the active site of an enzyme. The specific arrangement of amino acids in the active site, influenced by both the primary sequence and secondary structures such as alpha helices and beta sheets, is critical for enzyme-substrate interactions.
Shape of an enzyme specifically shape of its active site determines enzyme specificity .
Enzyme specificity is mainly determined by the active site structure and the interactions between the enzyme and its substrate. The shape, charge, and chemical properties of the active site are crucial in determining which substrates can bind to the enzyme and undergo a catalyzed reaction. Additionally, enzymes undergo conformational changes upon substrate binding to further enhance specificity.
What an enzyme does is based on its shape, therefore you would have to change it on a molecular level in order to alter its job.
The three-dimensional structure of trypsin determines the arrangement of its active site, which is crucial for its ability to bind to its substrate (protein) and catalyze the hydrolysis of peptide bonds efficiently. Any changes in the structure can alter the enzyme's specificity and activity, affecting its ability to function properly.
Yes.
ATP synthase is the protein enzyme involved in chemiosmosis. It is responsible for generating ATP by facilitating the movement of protons across the inner mitochondrial membrane.
True. Protein is an essential building material for cells. It is involved in many cellular processes, such as structure, signaling, and enzyme activity.
Enzyme specificity is mainly determined by the unique structure of their active site, which allows them to bind to specific substrates. This specificity arises from the unique sequence and conformation of amino acids that make up the active site, which are dictated by the enzyme's genetic code. Additionally, the 3D shape of enzymes is influenced by their environment, such as temperature and pH, which can affect their function and specificity.
No, kinesin is a motor protein involved in the movement of organelles and other cellular components along microtubules. It is not an enzyme.
Actually it is. It is a polypeptide structure that has been specialized to be a catalyst.
The size of the enzyme's active site would not contribute significantly to substrate specificity. Substrate specificity is typically determined by the shape, charge, and chemical properties of the active site that can properly bind to the substrate.
by function is enzyme ... by structure is hormone