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...

Quantitative relations in protein and RNA folding are deduced from the quantum folding theory of macromolecules. It includes: deduction of the law on the temperature-dependence of folding rate and its tests on protein dataset; study on the chain-length dependence of the folding rate for a large class of biomolecules; deduction of the statistical relation of folding free energy versus chain-leng...

Several proteins of the mitochondrial intermembrane space are targeted by internal targeting signals. A class of such proteins with α-helical hairpin structure bridged by two intramolecular disulfides is trapped by a Mia40-dependent oxidative process. Here, we describe the oxidative folding mechanism underpinning this process by an exhaustive structural characterization of the protein in all st...

A general theoretical framework is developed using free energy functional methods to understand the effects of heterogeneity in the folding of a well-designed protein. Native energetic heterogeneity arising from non-uniformity in native stability, as well as entropic heterogeneity intrinsic to the topology of the native structure are both investigated as to their impact on the folding free ener...

A general theoretical framework is developed using free-energy functional methods to understand the effects of heterogeneity in the folding of a well-designed protein. Native energetic heterogeneity arising from nonuniformity in native stabilizing interactions, as well as entropic heterogeneity intrinsic to the topology of the native structure, are both investigated as to their impact on the fo...

PDI catalyzes the oxidative folding of disulfide-containing proteins. However, the sequence of reactions leading to a natively folded and oxidized protein remains unknown. Here we demonstrate a technique that enables independent measurements of disulfide formation and protein folding. We find that non-native disulfides are formed early in the folding pathway and can trigger misfolding. In contr...

Folding mechanisms of proteins incorporated within supramolecular assemblies, including viruses, are little understood and may differ fundamentally from folding mechanisms of small globular proteins. We describe a novel Raman dynamic probe of hydrogen-isotope exchange to investigate directly these protein folding/assembly pathways. The method is applied to subunit folding in assembly intermedia...

Folding of Ubiquitin (Ub), a functionally important protein found in eukaryotic organisms, is investigated at low and neutral pH at different temperatures using simulations of the coarse-grained self-organized-polymer model with side chains (SOP-SC). The melting temperatures (Tm's), identified with the peaks in the heat capacity curves, decrease as pH decreases, in qualitative agreement with ex...

Image logs of 13 wells in the Rag Sefid Anticline show two systems of fractures developed under two deformation phase in the Dezful Embayment. This deformation phases are folding resulted from Zagros NE contraction and reactivation of the basement fault rotated the fold axial trace within the Hendijan-Izeh fault zone. Folding phase comprises four sets of fractures, which include axial and cross...

The elongated three-helix-bundle spectrin domains R16 and R17 fold and unfold unusually slowly over a rough energy landscape, in contrast to the homologue R15, which folds fast over a much smoother, more typical landscape. R15 folds via a nucleation-condensation mechanism that guides the docking of the A and C-helices. However, in R16 and R17, the secondary structure forms first and the two hel...