Rational design of thermally stable proteins: relevance to bionanotechnology.
Design of thermally stable proteins is spurred by their applications in bionanotechnology. There are three major issues governing this: first, the upper limit on the temperature at which proteins remain physiologically active and are available for technological applications (answers may emerge from the discovery of new, natural hyperthermophilic enzymes that are active above 125 degrees C or from the selection of mutants of hyperthermophilic enzymes that are more stable); second, the use of hyperthermophilic enzymes as molecular templates to design highly stable enzymes that have high activity at low temperatures; third, the link between rigidity and flexibility to thermostability and activity, respectively. We review progress in these areas.
Renugopalakrishnan
V
V
Children's Hospital, Harvard Medical School, Harvard University, Boston 02115, USA.
Garduño-Juárez
R
R
Narasimhan
G
G
Verma
C S
CS
Wei
X
X
Li
Pingzuo
P
D001436:Bacteriorhodopsins / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry*; D005288:Ferredoxins / Q000737:chemistry; D006358:Hot Temperature; D009154:Mutation; D036103:Nanotechnology / Q000379:methods*; D011487:Protein Conformation; D011489:Protein Denaturation; D015202:Protein Engineering; D012416:Rubredoxins / Q000737:chemistry; D012984:Software; D013696:Temperature; D013816:Thermodynamics
D004798:Enzymes; D005288:Ferredoxins; D012416:Rubredoxins; D001436:Bacteriorhodopsins