Many biological processes generate force, and proteins have evolved to resist and respond to tension along different force axes. Single-molecule force spectroscopy allows for molecular insight into the behavior of proteins under force and the mechanism of protein folding in general. Here, we have used src SH3 to investigate the effect of different pulling axes under the low-force regime afforde...

purpose : to determine the association between astigmatism and spherical refractive error in a clinical population methods : in this cross-sectional study, 2,000 patients who presented to our optometry clinic were enrolled. all were tested for objective refraction with a nidek ar-310a auto refractometer, and non-cycloplegic refraction. for those under 15 years of age, cycloplegic refraction was...

It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...

It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...

The folding patterns of the brain vary dramatically across species. Moreover, the location of sulcal (valley) and gyral (ridge) folds differ considerably in terms of their size, shape and extent even within a species. A paradigm for cortical pattern formation within or across species has not become apparent. Discussions as to how cortical folding patterns occur have recently emerged in the lite...

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...