Modification of the stability of phospholipase A2 by charge engineering

Electrostatic interactions play an important role in stabilizing the folded conformation of globular proteins. Here we predict the change in stability of charge engineered mutants, construct these mutants and compare the predicted change in stability with that observed. The change in stability was c...

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Veröffentlicht in:	FEBS letters 1991-04, Vol.281 (1), p.219-222
Hauptverfasser:	Pickersgill, Richard W., Sumner, Ian G., Collins, Margaret E., Warwicker, Jim, Perry, Barry, Bhat, K.Mahalingeshwara, Goodenough, Peter W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Charge engineering electrostatic properties Enzyme Stability Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Guanidine Guanidines Hydrogen-Ion Concentration Hydrolases Models, Molecular Mutagenesis phospholipase A2 Phospholipases A - chemistry Phospholipases A - genetics Phospholipases A2 pigs Protein Conformation Protein Denaturation Protein engineering of phospholipase A2 Protein stability Software stability X-Ray Diffraction
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Beschreibung
Zusammenfassung:	Electrostatic interactions play an important role in stabilizing the folded conformation of globular proteins. Here we predict the change in stability of charge engineered mutants, construct these mutants and compare the predicted change in stability with that observed. The change in stability was correctly predicted for two of the three mutants and the factors responsible for the discrepancy between observation and prediction for the third mutant are discussed.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(91)80397-L