Chemical Glycosylation: New Insights on the Interrelation Between Protein Structural Mobility, Thermodynamic Stability, and Catalysis.
From: Department of Chemistry, University of Puerto Rico, Río Piedras Campus, Facundo Bueso Bldg Lab-215, San Juan 23346, PR 00931-3346.
FEBS letters
- Publish Date: Mar 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 6
- Pages: 1685-90
- Medium: Print
- Language: English
- Citation (JAMA): Solá Ricardo J, Griebenow Kai, et al. Chemical Glycosylation: New Insights on the Interrelation Between Protein Structural Mobility, Thermodynamic Stability, and Catalysis.. FEBS Lett. Mar 2006;580:1685-90
Abstract
Chemical protein glycosylation was employed to sequentially modulate the structural dynamics of the serine protease alpha-chymotrypsin as evidenced from amide H/D exchange kinetics. The reduction in alpha-CT’s structural dynamics at increasing glycan molar contents statistically correlated with the increased thermodynamic stability (T(m)) and reduced rate of enzyme catalysis (k(cat)) exhibited by the enzyme upon chemical glycosylation. Temperature-dependent experiments revealed that native-like structural dynamics and function could be restored for the glycosylated conjugates at temperature values close to their thermodynamic stability suggesting that the concept of “corresponding states” can be extended to glycoproteins. These results demonstrate the value of chemical glycosylation as a tool for studying the role of protein structural dynamics on protein biophysical properties; e.g. enzyme stability and function.
Mesh Headings (Keywords): Animals, Catalysis, Cattle, Chymotrypsin, Glycosylation, Protein Conformation, Protein Folding, Proteins, Thermodynamics
Check for Full Text / PubMed Unique Identifier (PMID): 16494868
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