Fév 08 2017

Mutantelec: An In Silico mutation simulation platform for comparative electrostatic potential profiling of proteins.

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/791

Jan 29 2017

Multi-target Selection of Catalytic Antibodies wih β-lactamase Activity using Phage Display

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/783

Mai 28 2016

Biotype Characterization, Developmental Profiling, Insecticide Response and Binding Property of Bemisia tabaci Chemosensory Proteins: Role of CSP in Insect Defense.

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/775

Avr 26 2016

Protein elongation, co-translational folding and targeting

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/813

Avr 06 2016

Managing the protein folding demands in the endoplasmic reticulum of plants

Journal New Phytol. 2016 Mar 14. doi: 10.1111/nph.13915. [Epub ahead of print] Authors Liu JX, Howell SH. Abstract Endoplasmic reticulum (ER) stress occurs in plants during certain developmental stages or under adverse environmental conditions, as a result of the accumulation of unfolded or misfolded proteins in the ER. To minimize the accumulation of misfolded proteins …

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/833

Avr 05 2016

Effect of ELP Sequence and Fusion Protein Design on Concentrated Solution Self-Assembly

Authors Guokui Qin, Paola M. Perez, Carolyn E. Mills, and Bradley D. Olsen Journal Biomacromolecules. 2016 Mar 1. [Epub ahead of print] Abstract Fusion proteins provide a facile route for the purification and self-assembly of biofunctional protein block copolymers into complex nanostructures; however, the use of biochemical synthesis techniques introduces unexplored variables into the design …

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/800

Avr 05 2016

Ising Model Reprogramming of a Repeat Protein’s Equilibrium Unfolding Pathway

J Mol Biol. 2016 Mar 4. pii: S0022-2836(16)00138-8. doi: 10.1016/j.jmb.2016.02.022. [Epub ahead of print] C. Millership, J.J. Phillips, E.R.G. Main Abstract Repeat proteins are formed from units of 20–40 aa that stack together into quasi one-dimensional non-globular structures. This modular repetitive construction means that, unlike globular proteins, a repeat protein’s equilibrium folding and thus thermodynamic …

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/796

Avr 02 2016

A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding

Journal Nature Structural & Molecular Biology 23, 278–285 (1 April 2016) | doi:10.1038/nsmb.3182 Authors Lisa D Cabrita , Anaïs M E Cassaignau , Hélène M M Launay , Christopher A Waudby , Tomasz Wlodarski , Carlo Camilloni , Maria-Evangelia Karyadi , Amy L Robertson , Xiaolin Wang , Anne S Wentink , Luke S Goodsell …

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/839

Fév 05 2016

Converting bulk sugars into prebiotics: semi-rational design of a transglucosylase with controlled selectivity

Authors Tom Verhaeghe, Karel De Winter, Magali Berland, Rob De Vreese, Matthias D’hooghe, Bernard Offmann and Tom Desmet Journal Chem. Commun., 2016, 52, 3687-3689 DOI: 10.1039/C5CC09940D Abstract Despite the growing importance of prebiotics in nutrition and gastroenterology, their structural variety is currently still very limited. The lack of straightforward procedures to gain new products in …

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Lien Permanent pour cet article : http://www.bernardoffmann.fr/archives/756

Jan 26 2016

De Novo Proteins with Life-Sustaining Functions are Structurally Dynamic

Authors Murphy GS, Greisman JB, Hecht MH. Journal J Mol Biol. 2015 Dec 18. pii: S0022-2836(15)00699-3. doi: 10.1016/j.jmb.2015.12.008. [Epub ahead of print] Abstract Designing and producing novel proteins that fold into stable structures and provide essential biological functions are key goals in synthetic biology. In initial steps toward achieving these goals, we constructed a combinatorial …

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