Structural changes of a protein bound to a polyelectrolyte depend on the hydrophobicity and polymerization degree of the polyelectrolyte

Influence of polyelectrolytes of different chemical structure and degree of polymerization on aggregation and denaturation of the oligomeric enzyme glyceraldehyde-3-phosphate dehydrogenase has been studied to ascertain molecular characteristics of the polymer chains providing the efficient preventio...

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Veröffentlicht in:	Biochemistry (Moscow) 2010-04, Vol.75 (4), p.437-442
Hauptverfasser:	Stogov, S. V, Izumrudov, V. A, Muronetz, V. I
Format:	Artikel
Sprache:	eng
Schlagworte:	Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Calorimetry, Differential Scanning Denaturation Electrolytes Electrolytes - chemistry Enzymes Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) - chemistry Hydrophobic and Hydrophilic Interactions Kinetics Life Sciences Microbiology Molecular biology Monosaccharides Oligomers Phosphates Polyelectrolytes Polymerization Polymers Polymers - chemistry Protein Binding Protein Denaturation Proteins Sugars Sulfones - chemistry
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