'Lineweaver' presentation slideshows

ENZYMES KINETICS, INHIBITION, REGULATION

ENZYMES KINETICS, INHIBITION, REGULATION. Muhammad Jawad Hassan Assistant Professor Biochemistry. Michaelis-Menten kinetics. V 0 varies with [S]. V max approached asymptotically. V 0 is moles of product formed per sec. when [P] is low (close to zero time). E + S ?ES?E + P.

1.02k views • 53 slides

Chemical kinetics: accounting for the rate laws

Chemical kinetics: accounting for the rate laws. ?????? ??? ?? ? ??. The approach to equilibrium. Forward: A ? B Rate of formation of B = k r [A] Reverse: B ? A Rate of decomposition of B = k r ? [ B ]. Net r ate of formation of B = k r [A] ? k r ? [ B ].

924 views • 49 slides

Enzyme Catalysis

Enzyme Catalysis. SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk. Learning objectives Lecture 11. You should be able to use Lineweaver -Burk plots to calculate KM and Vmax You will be able to describe competitive,

593 views • 44 slides

Type of Inhibitors

The effect of inhibitor (Inorganic phosphate & Sodium fluoride) on the rate of an enzyme catalyzed reaction. Type of Inhibitors .

562 views • 25 slides

Enzyme Kinetics II

Enzyme Kinetics II. 10/16/2008. Kinetic data cannot unambiguously establish a reaction mechanism. Although a phenomenological description can be obtained the nature of the reaction intermediates remain indeterminate and other independent measurements are needed .

468 views • 22 slides

Figure 6.04 Effect of a catalyst on a chemical reaction.

316 views • 20 slides

Lecture 4

432 views • 17 slides