Some thermostable proteins are stabilized by an increased size of the protein’s hydrophobic core, an increased size of the interface between its domains and/or subunits, and a more tightly packed core as evidenced by a reduced surface-to-volume ratio.

TLS Online TPP Program

#Id: 4924

#XL - Q Biochemistry

TLS Online TPP Program

#Id: 4929

#XL - Q Biochemistry

Lineweaver-Burk plot showing the effect of uncompetitive inhibition; (b) the same, showing plots for several inhibitor concentrations at fixed enzyme concentration.

TLS Online TPP Program

#Id: 4932

#XL - Q Biochemistry

A non-competitive inhibitor can combine with an enzyme molecule to produce a dead-end complex.

TLS Online TPP Program

#Id: 4938

#XL - Q Biochemistry

TLS Online TPP Program

#Id: 8302

#XL - Q Biochemistry

TLS Online TPP Program

#Id: 8541

#XL - Q Biochemistry

The dependent variable is the rate of the reaction. 

The independent variables are the concentration of enzyme, the concentration of the substrate, the temperature, and the addition of an inhibitor