نتایج جستجو برای: hydrophobic support

تعداد نتایج: 688763  

Journal: :Journal of virology 2007
Jason Netland Debra Ferraro Lecia Pewe Heidi Olivares Thomas Gallagher Stanley Perlman

Severe acute respiratory syndrome coronavirus encodes several accessory proteins of unknown function. We previously showed that one such protein, encoded by ORF6, enhanced the growth of mouse hepatitis virus in tissue culture cells and in mice. Protein 6 consists of an N-terminal hydrophobic peptide and a C-terminal region containing intracellular protein sorting motifs. Herein, we show that mu...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2002
Margaret S Cheung Angel E García José N Onuchic

The interplay between structure-search of the native structure and desolvation in protein folding has been explored using a minimalist model. These results support a folding mechanism where most of the structural formation of the protein is achieved before water is expelled from the hydrophobic core. This view integrates water expulsion effects into the funnel energy landscape theory of protein...

2002
Margaret S. Cheung Angel E. Garcia Jose N. Onuchic

The interplay between structure-search of the native structure and desolvation in protein folding has been explored using a minimalist model. These results support a folding mechanism where most of the structural formation of the protein is achieved before water is expelled from the hydrophobic core. This view integrates water expulsion effects into the funnel energy landscape theory of protein...

2017
Florian Rohrbacher André Zwicky Jeffrey W. Bode

An antibacterial cyclic AS-48 protein was chemically synthesized by a-ketoacid–hydroxylamine (KAHA) ligation. Initial challenges associated with the exceptionally hydrophobic segments arising from the amphiphilic nature of the protein were resolved by the development of bespoke reaction conditions for hydrophobic segments, using hexafluoroisopropanol (HFIP) as a co-solvent. The synthetic protei...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1998
B A Schulman D L Lindstrom E Harlow

An important question in the cell cycle field is how cyclin-dependent kinases (cdks) target their substrates. We have studied the role of a conserved hydrophobic patch on the surface of cyclin A in substrate recognition by cyclin A-cdk2. This hydrophobic patch is approximately 35A away from the active site of cdk2 and contains the MRAIL sequence conserved among a number of mammalian cyclins. In...

Journal: :Protein science : a publication of the Protein Society 2012
Benjamin C Buer Jennifer L Meagher Jeanne A Stuckey E Neil G Marsh

Highly fluorinated analogs of hydrophobic amino acids are well known to increase the stability of proteins toward thermal unfolding and chemical denaturation, but there is very little data on the structural consequences of fluorination. We have determined the structures and folding energies of three variants of a de novo designed 4-helix bundle protein whose hydrophobic cores contain either hex...

Journal: :The Journal of biological chemistry 2011
Noel A Warfel Matt Niederst Alexandra C Newton

The pro-survival kinase Akt requires phosphorylation at two conserved residues, the activation loop site (Thr-308) and the hydrophobic motif site (Ser-473), for maximal activation. Previous reports indicate that mTORC2 is necessary for phosphorylation of the hydrophobic motif and that this site is not phosphorylated in cells lacking components of the mTORC2 complex, such as Sin1. Here we show t...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2010
Morten Ø Jensen David W Borhani Kresten Lindorff-Larsen Paul Maragakis Vishwanath Jogini Michael P Eastwood Ron O Dror David E Shaw

We present the first atomic-resolution observations of permeation and gating in a K(+) channel, based on molecular dynamics simulations of the Kv1.2 pore domain. Analysis of hundreds of simulated permeation events revealed a detailed conduction mechanism, resembling the Hodgkin-Keynes "knock-on" model, in which translocation of two selectivity filter-bound ions is driven by a third ion; formati...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2011
Phillip W Snyder Jasmin Mecinovic Demetri T Moustakas Samuel W Thomas Michael Harder Eric T Mack Matthew R Lockett Annie Héroux Woody Sherman George M Whitesides

The hydrophobic effect--a rationalization of the insolubility of nonpolar molecules in water--is centrally important to biomolecular recognition. Despite extensive research devoted to the hydrophobic effect, its molecular mechanisms remain controversial, and there are still no reliably predictive models for its role in protein-ligand binding. Here we describe a particularly well-defined system ...

Journal: :iranian journal of public health 0
fethi ben abdallah 1. laboratory of genetic, biodiversity and valorization of bio-ressources. higher institute of biotechnology , monastir, tunisia . ; 2. fermentation unit, pasteur institute , tunisia. rihab lagha 3. laboratory of analysis, treatment and valorization of environment polluants and product. faculty of pharmacy, monastir , tunisia. khaled said 1. laboratory of genetic, biodiversity and valorization of bio-ressources. higher institute of biotechnology , monastir, tunisia . héla kallel 2. fermentation unit, pasteur institute , tunisia. jawhar gharbi 4. sequencing and genomic analysis unit. higher institute of biotechnology , monastir, tunisia.

the aim of this study was to evaluate the ability of 15 serotypes of salmonella to form biofilm on polystyrene, polyvinyl chloride (pvc) and glass surfaces. .initially slime production was assessed on cra agar and hydrophobicity of 20 salmonella strains isolated from poultry and human and two salmonella enterica serovar typhimurium references strains was achieved by microbial adhesion to n-hexa...

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