The thermodynamic behavior of a three-dimensional off-lattice model for protein folding is probed. The model has only two types of residues, hydrophobic and hydrophilic. In absence of local interactions, native structure formation does not occur for the temperatures considered. By including sequence independent local interactions, which qualitatively reproduce local properties of functional pro...

The small helical protein BBL has been shown to fold and unfold in the absence of a free energy barrier according to a battery of quantitative criteria in equilibrium experiments, including probe-dependent equilibrium unfolding, complex coupling between denaturing agents, characteristic DSC thermogram, gradual melting of secondary structure, and heterogeneous atom-by-atom unfolding behaviors sp...

Fluorescence and circular dichroism stopped-flow have been widely used to determine the kinetics of protein folding including folding rates and possible folding pathways. Yet, these measurements are not able to provide spatial information of protein folding/unfolding. Especially, conformations of denatured states cannot be elaborated in detail. In this study, we apply the method of fluorescence...

The thermodynamic behavior of a three-dimensional oo-lattice model for protein folding is probed. The model has only two types of residues, hydrophobic and hydrophilic. In absence of local interactions , native structure formation does not occur for the temperatures considered. By including sequence independent local interactions, which qualitatively reproduce local properties of functional pro...

Anfinsen’s thermodynamic hypothesis is reviewed and misunderstandings are clarified. It really should be called the thermodynamic principle of protein folding. Energy landscape is really just the mathematical graph of the Gibbs free energy function ( ) X; , N G U E , a very high dimensional hyper surface. Without knowing it any picture of the Gibbs free energy landscape has no theoretical base,...

The rugged folding landscapes of functional proteins puts them at risk of misfolding and aggregation. Serine protease inhibitors, or serpins, are paradigms for this delicate balance between function and misfolding. Serpins exist in a metastable state that undergoes a major conformational change in order to inhibit proteases. However, conformational labiality of the native serpin fold renders th...

The thermodynamic behavior of a three-dimensional off-lattice model for protein folding is probed. The model has only two types of residues, hydrophobic and hydrophilic. In absence of local interactions, native structure formation does not occur for the temperatures considered. By including sequence independent local interactions, which qualitatively reproduce local properties of functional pro...

Protein folding mechanisms have remained elusive mainly because of the transient nature of intermediates. Leech-derived tryptase inhibitor (LDTI) is a Kazal-type serine proteinase inhibitor that is emerging as an attractive model for folding studies. It comprises 46 amino acid residues with three disulfide bonds, with one located inside a small triple-stranded antiparallel beta-sheet and with t...

The tropical tropopause layer (TTL) is a transition region between the troposphere and the stratosphere. In this study the vertical extent of the TTL is diagnosed from radiosonde and ozonesonde profiles in the tropics and a climatology of this layer is presented. The radiative balance in the TTL is also characterized. The TTL is locally defined as extending from the level of the lapse rate mini...

A ll life from viruses to blue whales relies on folding processes that can have fatal consequences when they go wrong. At the molecular level, folding is involved in DNA packaging and the fundamental process by which proteins assume their structural conformation and thereby function. At the cellular and tissue level, many plants depend on folding to prevent pollen grains from drying up through ...