Observatorio de I+D+i UPM

Descripción
Abstract: In the search for factors that make a protein allergenic (an issue that remains so far elusive) some common features of allergens such as small size, high stability and lipid binding are recognized in spite of their structural diversity. Other relevant but still poorly understood feature is their capability to form homodimers. We investigated by means of Molecular Dynamics (MD) calculations the stability in solution of several dimers of three major allergens from Alternaria mold, birch pollen, and peach fruit known to play essential roles in allergic disease. By running 20 ns MD simulations we found essential properties on solution that provide information of interest on their dimerization, stability of their epitopes and dynamical features of ligand binding cavities. Our results show that three essential allergen proteins display a distinct behavior on their trends to form homodimers in solution.
Internacional	Si
JCR del ISI	Si
Título de la revista	Molecular Informatics
ISSN	1868-1743
Factor de impacto JCR	2,013
Información de impacto
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DOI
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Desde la página	682
Hasta la página	694
Mes	SIN MES
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Esta actividad pertenece a memorias de investigación

• Autor: Maria Garrido Arandia (UPM)
• Autor: Araceli Diaz Perales (UPM)
• Autor: Luis Fernandez Pacios (UPM)
• Autor: Cristina Gomez Casado (UPM)

• Creador: Grupo de Investigación: Biotecnología Vegetal
• Departamento: Sistemas y Recursos Naturales
• Departamento: Biotecnología - Biología Vegetal