the use of organophosphorus hydrolase (oph) enzyme to degrade chemical warfare agents is one of the most frequently used decontamination methods. oph is a ~36 kda homodimeric metalloprotein that is found in the membrane of flavobacterium sp. strain atcc 27551 and brevundimonas diminuta mg and is capable of hydrolyzing a wide range of oxon and thion , such as paraoxon and parathion. oph gene ( o...

A new class of experiments that probe folding of individual protein domains uses mechanical stretching to cause the transition. We show how stretching forces can be incorporated in lattice models of folding. For fast folding proteins, the analysis suggests a complex relation between the force dependence and the reaction coordinate for folding.

background: rna plays key role in many aspects of biological processes and its tertiary structure is critical for its biological function. rna secondary structure represents various significant portions of rna tertiary structure. since the biological function of rna is concluded indirectly from its primary structure, it would be important to analyze the relations between the rna sequences and t...

Understanding how monomeric proteins fold under in vitro conditions is crucial to describing their functions in the cellular context. Significant advances in theory and experiments have resulted in a conceptual framework for describing the folding mechanisms of globular proteins. The sizes of proteins in the denatured and folded states, cooperativity of the folding transition, dispersions in th...

Proteins fold in a time range of microseconds to minutes despite the large amount of possible conformers. Molecular dynamics simulations of a three-stranded antiparallel beta-sheet peptide (for a total of 12.6 microsec and 72 folding events) show that at the melting temperature the unfolded state ensemble contains many more conformers than those sampled during a folding event.

Simple theoretical concepts and models have been helpful to understand the folding rates and routes of single-domain proteins. As reviewed in this article, a physical principle that appears to underly these models is loop closure.

A new approach to the interpretation of residual dipolar couplings for the regular secondary structures of proteins is presented. This paper deals with the analysis of the steric and chiral requirements of protein secondary structures and establishes a quantitative correlation between structure periodicity and the experimental values of the backbone residual dipolar couplings. Building on the r...

The extent to which glass-like kinetics govern dynamics in protein folding has been heavily debated. Here, we address the subject with an application of space-time perturbation theory to the dynamics of protein folding Markov state models. Borrowing techniques from the s-ensemble method, we argue that distinct active and inactive phases exist for protein folding dynamics, and that kinetics for ...

The early decades of Cell witnessed key discoveries that coalesced into the field of chaperones, protein folding, and protein quality control.

This review summarises our current understanding of the underlying and universal mechanism by which newly synthesised proteins achieve their biologically functional states. Protein molecules, however, all have a finite tendency either to misfold, or to fail to maintain their correctly folded states, under some circumstances. This article describes some of the consequences of such behaviour, par...