Enzymatic turnovers of single cholesterol oxidase molecules were observed in real time by
monitoring the emission from the enzyme's fluorescent active site, flavin adenine …

Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme
motions linked to substrate turnover remain largely unknown. We have studied dynamics of …

By simultaneous analysis of the on-time distribution and autocorrelation function of a single
working cholesterol oxidase enzyme, a diffusional model reveals the coupling of …

Published by AAAS achieve a sophisticated series of changes in structure and dynamics.
According to this view, for each state along the enzymatic cycle of dihydrofolate reductase …

Single-molecule techniques offer a unique tool for studying the dynamical behavior of
individual molecules and provide the possibility to construct distributions from individual …

Individual enzyme molecules have been observed to possess discrete and different turnover
rates due to the presence of long-lived activity states. These stable activity states are thought …

Conformational dynamics play a key role in enzyme catalysis. Although protein motions
have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme …

The study of single molecules is a relatively new field of research but covers a wide range of
systems from dilute gases to complex biological systems. A recent issue of Accounts of …

Recent single-molecule enzymology measurements with improved statistics have
demonstrated that a single enzyme molecule exhibits large temporal fluctuations of the …

INTRODUCTION Enzymes greatly accelerate biochemical reactions by providing a scaffold
to bind and recognize substrate, position catalytic units, and facilitate the formation of …