Segundo Simposio
sobre Proteínas
Plegamiento
México

Octubre 19-21 2005

Ciudad

Universitaria

.

Registro

.

José M. Sanchez Ruíz

Facultad de Ciencias, Departamento de Química Física, Universidad de Granada, 18071-Granada, España

correo-e: ajsj@ssk.es

Licenciado en Química, Universidad de Granada (España). 1979.
Doctor en Química Física. Universidad de Granada, 1983.
Fulbright Scholar: 1984-1986. The Medical College of Virginia (USA).
Posición actual: Catedrático de Química Física, Universidad de Granada.
Miembro del Consejo Editorial de Biophysical Chemistry.

Campos de interés:
Relación estructura-energética en macromoléculas biológicas. Plegamiento de proteínas. Contribuciones electrostáticas a la estabilidad de las proteínas. Diseño racional de proteínas. Estructura residual en estados desnaturalizados. Evolución molecular.

Conferencia
Caracterización del desplegamiento de proteínas por Calorimetría Diferencial de Barrido: la energética de la estabilidad de proteínas y el plegamiento downhill

Resumen
Differential Scanning Calorimetry (DSC) has a long history of interesting and useful applications in the field of protein energetics (and also, in the energetic analysis of other biological systems). In fact, DSC studies on protein thermal denaturation have played a central role in the development of current views about the factors that determine protein stability. Reviews on the various aspects of this technique are available in the literature. It may appear, therefore, that DSC cannot be considered as an "emerging technique" in any sense of the word. However, there have been several recent developments in DSC of proteins that merit a special consideration. First and foremost, recent studies (in which DSC has been instrumental) have provided evidence for the downhill (barrierless) character of the folding process for some small proteins. Needless to say, the existence of downhill folding (and the possibility that it may be detected by DSC) may have a huge influence in future studies on protein folding and stability. In addition, studies published in the last few years have made apparent that DSC can be used to probe complex processes involving, for instance, interactions of proteins with other molecules or cooperative changes in protein denatured states. In this talk I will describe in some detail these and other "emerging applications" of DSC, although I will also provide a short, general introduction to the technique.

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