By Mukesh Doble
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Extra resources for Biotransformation and Bioprocesses (BIOTECHNOLOGY AND BIOPROCESSING SERIES)
Van der Waals forces arise when unbalanced electrical charges around molecules attract one another. Though the charges are always ﬂuctuating and even reversing direction, the net eﬀect is to draw two molecules together. , (1) London dispersion forces, which arise due induced dipole–induced dipole or in other words instantaneous dipole caused due to the ﬂuctuating movement of electrons in an atom resulting in a deformation of the electron cloud of the atom approaching close to it, (2) Debye forces, which arise due to dipole– induced dipole interaction.
Since the peptide units are eﬀectively rigid groups that are linked into a chain by covalent bonds at the Ca atoms, the only degrees of freedom they have are rotations around the CaUC and the NUCa bonds. A convention has been adopted to call the angle of rotation around NUCa bond phi (f) and angle around the CaUC1 bond psi (c). In this way each amino acid residue is associated with two conformational angles f and c. Since these are the only degrees of freedom, the conformation of the whole main chain of the polypeptide (protein) is completely determined when the f and c angles for each amino acid are deﬁned.
2 Active Site It is known that the substrate binds to a speciﬁc region of the enzyme called the active site, where reaction occurs and products are released. The interactions between the substrate and the enzyme are due to hydrogen bonding and van der Waal interaction. In heterogeneous catalysis the substrate is chemisorbed on the catalyst site due to pi-bond interaction between the substrate and the metal atoms. The size of the active metal sites are of the order of microns whereas that of enzymes is in the range of 50-100 A˚.
Biotransformation and Bioprocesses (BIOTECHNOLOGY AND BIOPROCESSING SERIES) by Mukesh Doble