نتایج جستجو برای: folding mechanism

تعداد نتایج: 590973  

Journal: :Physical review letters 2004
B Oztop M R Ejtehadi S S Plotkin

By observing trends in the folding kinetics of experimental 2-state proteins at their transition midpoints, and by observing trends in the barrier heights of numerous simulations of coarse-grained, C(alpha) model Go proteins, we show that folding rates correlate with the degree of heterogeneity in the formation of native contacts. Statistically significant correlations are observed between fold...

Journal: :Biochemistry and Biophysics Reports 2017

Journal: :IOP Conference Series: Materials Science and Engineering 2020

Journal: :Biochemistry 2005
D Thirumalai Changbong Hyeon

Visualizing the navigation of an ensemble of unfolded molecules through the bumpy energy landscape in search of the native state gives a pictorial view of biomolecular folding. This picture, when combined with concepts in polymer theory, provides a unified theory of RNA and protein folding. Just as for proteins, the major folding free energy barrier for RNA scales sublinearly with the number of...

2014
Lee Gyan Kwa Beth G. Wensley Crispin G. Alexander Stuart J. Browning Benjamin R. Lichman Jane Clarke

Three homologous spectrin domains have remarkably different folding characteristics. We have previously shown that the slow-folding R16 and R17 spectrin domains can be altered to resemble the fast folding R15, in terms of speed of folding (and unfolding), landscape roughness and folding mechanism, simply by substituting five residues in the core. Here we show that, by contrast, R15 cannot be en...

2006
R.D.M. Travasso P.F.N. Faisca M. M. Telo da Gama

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...

Journal: :Journal of molecular biology 2005
Diego U Ferreiro Samuel S Cho Elizabeth A Komives Peter G Wolynes

Proteins consisting of repeating amino acid motifs are abundant in all kingdoms of life, especially in higher eukaryotes. Repeat-containing proteins self-organize into elongated non-globular structures. Do the same general underlying principles that dictate the folding of globular domains apply also to these extended topologies? Using a simplified structure-based model capturing a perfectly fun...

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