Modulation of buried ionizable groups in proteins with engineered surface charge.
Recent work has shown that proteins can tolerate hydrophobic-to-ionizable-residue mutations. Here, we provide experimental evidence that the essential properties (pK value, protonation state, local dynamics) of buried ionizable groups in proteins can be efficiently modulated through the rational design of the surface charge distribution, thus paving the way for the protein engineering exploitation of charge burial.
Pey
Angel L
AL
Facultad de Ciencias, Departamento de Quimica Fisica, Universidad de Granada, 18071-Granada, Spain.
Rodriguez-Larrea
David
D
Gavira
Jose A
JA
Garcia-Moreno
Bertrand
B
Sanchez-Ruiz
Jose M
JM
D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics; D007477:Ions / Q000737:chemistry*; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D055672:Static Electricity; D013816:Thermodynamics; D013879:Thioredoxins / Q000737:chemistry / Q000235:genetics
D029968:Escherichia coli Proteins; D007477:Ions; D011506:Proteins; D013879:Thioredoxins