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BIO731 PAST PAPERS
BIO731 PAST PAPERS
CS201 FINAL TERM SOLVED PAPERS BY WAQAR SIDHU. ENG101 FINAL TERM SOLVED MCQS. CS403 CURRENT FINAL TERM PAPERS. CS101 FINAL TERM SOLVED PAPERS BY MOAAZ MEGA FILE. CS201 FINAL TERM SOLVED PAPERS BY MOAAZ MEGA FILE. CS205 FINAL TERM PAST PAPERS. CS204 FINAL TERM PAST PAPERS. CS301 FINAL TERM SOLVED PAPERS BY MOAAZ. CS304 FINAL TERM SOLVED PAPERS BY MOAAZ. CS311 FINAL TERM SOLVED PAPERS BY MOAAZ. CS401 FINAL TERM SOLVED PAPERS BY MOAAZ
Changes in enzyme form due to non-competitive inhibition
An example of allosteric is (elo-, “other”;
“Form”). In that case, the binding of the inhibitor is indicated
Protein to change its shape. enzymes are the most common
The inactive form of the enzyme has a non-binding form
Molecular, when the active form has the correct shape
Active site for attaching the substrate to the legs.
These two forms may interact, and this process is controlled by binding of an allosteric regulator to an enzyme site away from the active site. The bonding regulator is similar to substrate bonding: it
very specific. So an enzyme can have multiple positions
is: one for the substrate(s) and the other for the controllers.
Allosteric regulators work in two ways:
Positive regulators confirm the active form of the enzyme.
Negative controllers stabilize the passive form
Most (but not all) enzymes are fully regulated
proteins with quaternary structure; ie they are made
up to several polypeptide subgroups.
The active site is in a subgroup called the catalytic subgroup, while the regulatory base(s) are in different subgroups, the regulatory subgroups.
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