نتایج جستجو برای: Folding state

تعداد نتایج: 881953  

Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...

ژورنال: گلجام 2014
زمانی, شادی, مجابی, سید علی,

One of the most common procedures for exporting and warehousing handmade carpets is keeping them folded over one another. Handmade carpets come out of their stable states by being folded,while increasing storage time can cause serious and sometimes irreversible changes to them. In this research, a pilot model carpet has kept folded under a load equal to 50 g/cm2 and then the applied load increa...

Journal: :biomacromolecular journal 2015
faizan ahmad sobia zaidi md imtaiyaz hassan asimul islam

cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. more than 280 sequences have been reported in the protein sequence database (www.uniprot.org). though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. thus a vast data set of varied sequences with retention of similar structure and function makes it a primary ca...

Journal: :The journal of physical chemistry. B 2005
Alberto Stizza Emidio Capriotti Mario Compiani

A diffusion-collision-like model is proposed for helical proteins with three-state folding dynamics. The model generalizes a previous scheme based on the dynamics of putatively essential parts of the protein (foldons) that was successfully tested on proteins with two-state folding. We show that the extended model, unlike the original one, allows satisfactory calculation of the folding rate and ...

Journal: :Protein science : a publication of the Protein Society 2014
Camille Lawrence Alexis Vallée-Bélisle Shawn H Pfeil Derek de Mornay Everett A Lipman Kevin W Plaxco

The folding of larger proteins generally differs from the folding of similarly large nucleic acids in the number and stability of the intermediates involved. To date, however, no similar comparison has been made between the folding of smaller proteins, which typically fold without well-populated intermediates, and the folding of small, simple nucleic acids. In response, in this study, we compar...

1998
KAZUMOTO IGUCHI K. Iguchi

I study the conceptual framework of protein folding considering an exactly solvable model — the Rubik’s magic snake model. I discuss the mathematical representation of the model, the model Levinthal paradox, the non-unique compact folded structure, the function of the chain, the ground state energy, the commensurability between the folded structure and the potential sequence, the relationship b...

Journal: :iranian journal of biotechnology 2014
javad mohammadzadeh mohammad ganjtabesh abbas nowzari-dalini

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...

Journal: :Journal of molecular biology 2003
Andrew I Jewett Vijay S Pande Kevin W Plaxco

The relative folding rates of simple, single-domain proteins, proteins whose folding energy landscapes are smooth, are highly dispersed and strongly correlated with native-state topology. In contrast, the relative folding rates of small, Gō-potential lattice polymers, which also exhibit smooth energy landscapes, are poorly dispersed and insignificantly correlated with native-state topology. Her...

1998
S. WALTER ENGLANDER TOBIN R. SOSNICK LELAND C. MAYNE MARK SHTILERMAN PHOEBE X. QI YAWEN BAI

A number of puzzling characteristics appear repeatedly in protein folding studies. Some proteins fold in a fast two-state manner with no apparent intermediates while others fold much more slowly in a multistate way. Many proteins fold heterogeneously; within the same controlled experiment some fraction of the population reaches the native state rapidly and others more slowly. These contradictor...

Journal: :The journal of physical chemistry. B 2013
Nan-jie Deng Wei Dai Ronald M Levy

Understanding how kinetics in the unfolded state affects protein folding is a fundamentally important yet less well-understood issue. Here we employ three different models to analyze the unfolded landscape and folding kinetics of the miniprotein Trp-cage. The first is a 208 μs explicit solvent molecular dynamics (MD) simulation from D. E. Shaw Research containing tens of folding events. The sec...

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