Protein folding research stalled for decades because conventional experiments indicated
that proteins fold slowly and in single strokes, whereas theory predicted a complex interplay …

A thermodynamically and kinetically simple picture of protein folding envisages only two
states, native (N) and unfolded (U), separated by a single activation free energy barrier, and …

DNA damage repair starts with the recognition of damaged sites from predominantly normal
DNA. In eukaryotes, diverse DNA lesions from environmental sources are recognized by the …

Insulin homodimer associates through the coupled folding and binding of two partially
disordered monomers. We aim to understand this dynamics by observing insulin dimer …

Mathematical models of degradation-relaxation kinetics are considered for jammed thick-film
systems composed of screen-printed spinel Cu 0.1 Ni 0.1 Co 1.6 Mn 1.2 O 4 and conductive …

Single-molecule fluorescence microscopy techniques can be used in combination with
micrometer length-scale temperature control and Förster resonance energy transfer (FRET) …

The presence and extent of hydrogen-bonding (H-bonding) cooperativity in proteins remains
a fundamental question, which in the past has been studied extensively, mostly by infrared …

A major goal of protein folding studies is to understand the structural basis of the coupling
between stabilizing interactions, which leads to cooperative conformational change. The …

Salt–bridge interactions play an important role in stabilizing many protein structures, and
have been shown to be designable features for protein design. In this work, we study the …

This paper analyzes the effect of pH on thermodynamic stability, low-frequency local motions
and microsecond folding kinetics of carbonmonoxycytochrome c (Cyt-CO) all across the …