The traditional view that partly folded intermediates are important for directing a protein
toward the native state has been challenged by the notion that proteins can intrinsically fold …

Globular proteins often exhibit cooperative unfolding transitions in which only folded (native)
and unfolded (denatured) molecules are populated at equilibrium. 1, 2 This two-state …

The success of fluorescence experiments requires attention to experimental details and an
understanding of the instrumentation. There are also many potential artifacts that can distort …

Discussions of biochemical fluorescence frequently start with the subject of protein
fluorescence. This is because, among biopolymers, proteins are unique in displaying useful …

Fluorescence spectroscopy and its multiple applications to protein analysis, and to the life
sciences in general, have undergone rapid development during the past decade. This …

The overall structure of the transition-state and intermediate ensembles observed
experimentally for dihydrofolate reductase and interleukin-1β can be obtained by using …

Interaction of bovine serum albumin (BSA) with two series of dipolar molecules having both
rigid and flexible structures has been studied by monitoring the spectral and temporal …

Time-resolved fluorescence spectroscopy is used to monitor molecular interactions and
motions that occur in the picosecond—nanosecond time range, and is especially useful in …

Various conformational states of polypeptide chains were investigated by synchrotron small-
angle X-ray scattering (SAXS). SAXS patterns of proteins and model polypeptides in …

The rates at which biological interactions occur can provide important information
concerning the mechanism and behavior of these processes in living systems. This review …