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Personen: Schubert, F. (Autor) 
Zettl, H. (Autor) 
H√§fner, W. (Autor) 
Krauss, G. (Autor) 
Krausch, Georg (Autor) 
  
Titel: Comparative thermodynamic analysis of dna-protein interactions using surface plasmon resonance and fluorescence correlation spectroscopy
  
Quelle: Biochemistry. Bd. 42. H. 34. Washington : American Chemical Society. S. 10288 - 10294
Erscheinungsjahr:    2003
ISBN / ISSN: 0006-2960
URL der Originalveröffentlichung doi:10.1021/bi034033d
  
Dokumentart:
Zeitschriftenaufsatz Zeitschriftenaufsatz
Sprache: Englisch
Open Access:
Person der Universität:   
Einrichtung: Universitätsleitung
DDC-Sachgruppe:    Physik
ID: 11496  Universitätsbibliothek Mainz
Hinweis:
Informationen zu den Nutzungsrechten unserer Inhalte Informationen zu den Nutzungsrechten unserer Inhalte
Abstract: We report a kinetic and thermodynamic analysis of interactions between ssDNA and replication protein A (RPA) using surface plasmon resonance (SPR) and fluorescence correlation spectroscopy (FCS) at variable temperature. The two methods yield different values for the Gibbs free energy but nearly the same value for the reaction enthalpy of ssDNA-RPA complex formation. The Gibbs free energy was determined by SPR and FCS to be -62.6 and -54.7 kJ/mol, respectively. The values for the reaction enthalpy are -64.4 and -66.5 kJ/mol. It is concluded that the difference in Gibbs free energy measured by the two methods is due to different reaction entropies. The entropic contribution to the free energy at 25 degreesC is -1.8 kJ/mol for SPR and -11.8 kJ/mol for FCS. In SPR, the reaction is restricted to two dimensions because of immobilization of the DNA molecules to the sensor surface. In contrast, FCS is able to follow complex formation without spatial restrictions. In consequence, the reaction entropy determined from SPR experiments is lower than for FCS experiments.
   
  
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