نتایج جستجو برای: accordingly have set his book mafatihol hayat

تعداد نتایج: 3562044  

Journal: :The Australian Library Journal 2007

Journal: :Journal of Hindu-Christian Studies 1996

Journal: :Applied and environmental microbiology 2004
Dong Soo Hwang Hyo Jin Yoo Jong Hyub Jun Won Kyu Moon Hyung Joon Cha

Mussel adhesive proteins have been suggested as a basis for environmentally friendly adhesives for use in aqueous conditions and in medicine. However, attempts to produce functional and economical recombinant mussel adhesive proteins (mainly foot protein type 1) in several systems have failed. Here, the cDNA coding for Mytilus galloprovincialis foot protein type 5 (Mgfp-5) was isolated for the ...

2015
Yongsheng Yu Jianpeng Wang Jiahui Liu Daishun Ling Jiang Xia

Natural proteins are often confined within their local microenvironments, such as three-dimensional confinement in organelles or two-dimensional confinement in lipid rafts on cytoplasmic membrane. Spatial confinement restricts proteins' entropic freedom, forces their lateral interaction, and induces new properties that the same proteins lack at the soluble state. So far, the phenomenon of envir...

2013
Heide Kogelberg Enrique Miranda Jerome Burnet David Ellison Berend Tolner Julie Foster Carmen Picón Gareth J. Thomas Tim Meyer John F. Marshall Stephen J. Mather Kerry Chester

The αvβ6 integrin is up-regulated in cancer and wound healing but it is not generally expressed in healthy adult tissue. There is increasing evidence that it has a role in cancer progression and will be a useful target for antibody-directed cancer therapies. We report a novel recombinant diabody antibody fragment that targets specifically αvβ6 and blocks its function. The diabody was engineered...

2017

We previously expressed VbhTA constructs for lysate AMPylation assays from the pRSFDuet-1 backbone, a plasmid with two multiple cloning sites that each enable the expression of constructs from a PT7 promoter. Our constructs encoded either the VbhT toxin alone (with an N-terminal hexahistidine (His6-)tag) to be expressed from the first multiple cloning site or had additionally the VbhA antitoxin...

Journal: :The Journal of General Physiology 2001
Michael Gordon Alan Finkelstein

In the presence of a low pH environment, the channel-forming T domain of diphtheria toxin undergoes a conformational change that allows for both its own insertion into planar lipid bilayers and the translocation of the toxin's catalytic domain across them. Given that the T domain contributes only three transmembrane segments, and the channel is permeable to ions as large as glucosamine(+) and N...

Journal: :Biotechnology progress 2005
Dong Soo Hwang Youngsoo Gim Hyung Joon Cha

Mussel adhesive proteins, including the 20-plus variants of foot protein type 3 (fp-3), have been suggested as potential environmentally friendly adhesives for use in aqueous conditions and in medicine. Here we report the novel production of a recombinant Mytilus galloprovincialis foot protein type 3 variant A (Mgfp-3A) fused with a hexahistidine affinity ligand in Escherichia coli and its appr...

Journal: :Analytical chemistry 2006
Farid Khan Mingyue He Michael J Taussig

There is a particular need in protein analysis and purification for specific, functional, and generic methods of protein immobilization on solid supports. Here we describe a double-hexahistidine (His6) tag sequence, comprising two hexahistidines separated by an 11-amino acid spacer, which shows at least 1 order of magnitude stronger binding to Ni-NTA-modified surfaces than a conventional single...

Journal: :The Yale Journal of Biology and Medicine 1943
Arturo Castiglioni

HE FIGHT for and against Vesalius began almost immediately after the publication of the Fabrica. It was characterized by two facts: the i first, that many of Vesalius' followers adopted his ideas, plagiarizing his book, badly reproducing the anatomical illustrations and sometimes suppressing his name, often presenting the whole-as a new interpretation of Galen's anatomy; the second, that the at...

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