Ontology highlight
ABSTRACT:
SUBMITTER: Varriale A
PROVIDER: S-EPMC3672191 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Varriale Antonio A Marabotti Anna A Mei Giampiero G Staiano Maria M D'Auria Sabato S
PloS one 20130604 6
In this work, we used a combination of fluorescence correlation spectroscopy (FCS) and molecular dynamics (MD) simulation methodologies to acquire structural information on pH-induced unfolding of the maltotriose-binding protein from Thermus thermophilus (MalE2). FCS has emerged as a powerful technique for characterizing the dynamics of molecules and it is, in fact, used to study molecular diffusion on timescale of microsecond and longer. Our results showed that keeping temperature constant, the ...[more]