Protein-Ligand Interactions mutations

Mutant Control for the effect of the mutation Experimental condition to probe the functional consequences of the protein-ligand interaction... 

UCW = capped water, TW = tethered water (see text), k = force constant for restraining potential (kcal/mol/A2). b Radius (A) of solvation sphere. 1 Numbers of dynamical water molecules within solvation sphere. d Mean and standard error for the forward (i.e. 8-methyl-N5-deazapterin —> 8-methylpterin) and reverse mutation of the electrostatic force field Cutoff for protein-ligand and solvent-ligand interaction all other interactions are subject to a 9 A cutoff. 

Randomization, however, does not always imply random mutation positions. Where there is prior knowledge of the protein s structure or specific functional residues (e.g., the active site of an enzyme or the ligand-interaction site of a receptor), this information can be used for identifying sites for selective randomization (see also Part III, Chapter 6). Several protocols have been established that allow the randomization of such sites or regions. Most protocols are based on oligonucleotides bearing the respective randomized positions. For an application of such protocols, see elsewhere (e.g., [24]) (see also Part V, Chapter 2). 

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