For the vast majority of naturally occurring, small, single domain proteins folding is often described as a two-state process that lacks detectable intermediates. This observation has often been rationalized on the basis of a nucleation mechanism for protein folding whose basic premise is the idea that after completion of a specific set of contacts forming the so-called folding nucleus the nati...

Recent experiments have conclusively shown that proteins are able to fold from an unknotted, denatured polypeptide to the knotted, native state without the aid of chaperones. These experiments are consistent with a growing body of theoretical work showing that a funneled, minimally frustrated energy landscape is sufficient to fold small proteins with complex topologies. Here, we present a theor...

Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases. Protein folding is a highly heterogeneous process and rarely populated intermediate states may play an important role. Single-molecule techniques are ideally suited to resolve these heterogeneities. In this thesis, I ...

In recent years, a growing number of protein folding studies have focused on the unfolded state, which is now recognized as playing a major role in the folding process. Some of these studies show that interactions occurring in the unfolded state can significantly affect the stability and kinetics of the protein folding reaction. In this study, we modeled the effect of electrostatic interactions...

Definition of the unfolded state of proteins is essential for understanding their stability and folding on biological timescales. Here, we find that under near physiological conditions the configurational ensemble of the unfolded state of the simplest protein structure, polyalanine alpha-helix, cannot be described by the commonly used Flory random coil model, in which configurational probabilit...

     Lali sub-surface structure, with a NW-SE Zagros trending is located in Dezful Embayment. To determine the folding mechanism, structural geometric parameters including limbs dip, amplitude, wavelength, and crestal length were determined in four stages during deformation. In order to investigate the lateral folding mechanism, these geometric parameters were analyzed in three parts in the Lal...

BACKGROUND Kinase-inducible domain (KID) as transcriptional activator can stimulate target gene expression in signal transduction by associating with KID interacting domain (KIX). NMR spectra suggest that apo-KID is an unstructured protein. After post-translational modification by phosphorylation, KID undergoes a transition from disordered to well folded protein upon binding to KIX. However, th...

Kinetic and equilibrium studies of the folding and unfolding of the SH3 domain of the PI3 kinase, have been used to identify a folding intermediate that forms after the rate-limiting step on the folding pathway. Folding and unfolding, in urea as well as in guanidine hydrochloride (GdnHCl), were studied by monitoring changes in the intrinsic fluorescence or in the far-UV circular dichroism (CD) ...

Buckle folds are common traps for hydrocarbon in several contractional provinces. Buckle folds form where stratified sequences rest a top salt or some other utterly weak rock as a decollemet zone in units with high competency contrasts by a compressive stress which acted along the length of the rock layers. An important parameter affecting buckle folding of a competent zone above a mobile decol...

The assembly of biological molecules, most notably globular proteins1 and RNA,2,3 into unique threedimensional structures with well-defined topology is a complex and fascinating phenomenon in molecular biology. There are two aspects to the problem of folding of proteins and RNA. The first is the prediction of the three-dimensional structure of the folded state from the one-dimensional primary s...