Deletions reveals sequence segments nonessential for proper folding of B. Licheniformis beta-lactamase.

RAUL GABRIEL FERREYRA; LEOPOLDO G GEBHARD; VALERIA A RISSO; JAVIER SANTOS; MARIO R. ERMACORA; MARTÍN E NOGUERA

Mar del Plata

Congreso; XXXIII Reunión Anual de Sociedad Argentina de Biofísica conjuntamente con Congreso Conjunto de Sociedades Biomédicas de la Argentina; 2004

Sociedades Biomédicas de la Argentina

A large body of convincing evidence indicates that not all residues in a protein are equally important for the acquisition of the native structure. Whereas some positions within a sequence tolerate multiple changes, others cannot be modified without drastically altering folding or stability. The importance of a sequence segment in determining protein folding can be examined by engineering deletions in a polypeptide chain. Therefore, the content of conformational information can be mapped into the sequence. Several truncated mutants of beta‑lactamase, a middle‑size protein with intermediate topological complexity, were prepared in order to examine the functional and structural role of different parts of the sequence. This approach identified regions of the sequence that are non-essential for proper folding.