IQUIBICEN   23947
INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CIENCIAS EXACTAS Y NATURALES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
NGOME: prediction of non-enzymatic protein deamidation from sequence-derived secondary structure and intrinsic disorder
Autor/es:
LORENZO, JR; ALONSO, LG; SÁNCHEZ IE
Reunión:
Conferencia; 10th Benelux Bioinformatics Conference; 2015
Resumen:
Asparagine residues in proteins undergo spontaneous deamidation, a post-translational modification that may act as a molecular clock for the regulation of protein function and turnover. Asparagine deamidation is modulated by protein local sequence, secondary structure and hydrogen bonding. We present NGOME, an algorithm able to predict non - enzymatic deamidation of internal asparagine residues in proteins, in the absence of structural data, from sequence based predictions of secondary structure and intrinsic disorder. NGOME may help the user identify deamidation-prone asparagine residues, often related to protein gain of function, protein degradation or protein misfolding in pathological processes.