Thermal and pH-Induced Conformational Changes of a β-Sheet Protein Monitored by Infrared Spectroscopy

The stability of a lentil lectin, an all-β protein, has been perturbed by changes in pH and temperature. In the pH interval 5.0 → 10.0, the overall secondary structure does not undergo significant changes. However, if the individual components of the infrared amide I band are considered, changes in...

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Veröffentlicht in:	Biochemistry (Easton) 1999-02, Vol.38 (5), p.1525-1530
Hauptverfasser:	Chehín, Rosana, Iloro, Ibón, Marcos, María José, Villar, Enrique, Shnyrov, Valery L, Arrondo, José Luis R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides - chemistry Fabaceae Hot Temperature Hydrogen-Ion Concentration Lectins - chemistry Plant Lectins Plant Proteins - chemistry Plants, Medicinal Protein Conformation Protein Denaturation Protein Structure, Secondary Spectroscopy, Near-Infrared
Online-Zugang:	Volltext
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