Stability, activity and flexibility in α-lactalbumin

α-Lactalbumins and the type-c lysozymes are homologues with similar folds that differ in function and stability. To determine if the lower stability of α-lactalbumin results from specific substitutions required for its adaptation to a new function, the effects of lysozyme-based and other substitutio...

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Veröffentlicht in:	Protein engineering 1999-07, Vol.12 (7), p.581-587
Hauptverfasser:	Greene, Lesley H., Grobler, Jay A., Malinovskii, Vladimir A., Tian, Jie, Acharya, K. Ravi, Brew, Keith
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Cattle Circular Dichroism Escherichia coli - metabolism flexibility Lactalbumin - chemistry Lactalbumin - genetics Lactalbumin - metabolism lactose synthase lysozyme Models, Molecular Molecular Sequence Data Mutation Protein Conformation Protein Folding protein structure Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid Structure-Activity Relationship thermal stability α-lactalbumin
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