Sanna Jääskeläinen, Chandra Verma, Roderick E. Hubbard, Pekka Lestko, Leo S. D. Caves,
Abstract The interfacial activation of Rhizomucor miehei lipase (RmL) involves the motion of an α‐helical region (residues 82‐96) which acts as a “lid” over the active site of the enzyme, undergoing a displacement from a “closed” to an “open” conformation upon binding of substrate. Normal mode analyses performed in both low and high dielectric media reveal that low‐frequency vibrational modes contribute significantly to the conformational transition between the closed and open conformations. In these ...
Tópico(s): Protein Structure and Dynamics
1998 - Wiley | Protein Science