نتایج جستجو برای: پورین ompf

تعداد نتایج: 704  

Journal: :The Biochemical journal 2003
Jérôme Bredin Valérie Simonet Ramkumar Iyer Anne H Delcour Jean-Marie Pagès

The L3 loop is an important feature of the OmpF porin structure, contributing to both channel size and electrostatic properties. Colicins A and N, spermine, and antibiotics that use OmpF to penetrate the cell, were used to investigate the structure-function relationships of L3. Spermine was found to protect efficiently cells expressing wild-type OmpF from colicin action. Among other solutes, su...

2017

Bacterial resistance is a critical public health issue and the development of alternative antibiotics to counteract this problem is an urgent matter. Fluoroquinolones are widely used antibiotics and numerous cases of bacterial resistance to these drugs have already been reported. One important mechanism of resistance is the decrease of the permeability of the bacterial membrane to antibiotics b...

Journal: :Biophysical journal 2002
Tatiana K Rostovtseva Ekaterina M Nestorovich Sergey M Bezrukov

To understand the physics of polymer equilibrium and dynamics in the confines of ion channel pores, we study partitioning of poly(ethylene glycol)s (PEGs) of different molecular weights into the bacterial porin, OmpF. Thermodynamic and kinetic parameters of partitioning are deduced from the effects of polymer addition on ion currents through single OmpF channels reconstituted into planar lipid ...

Journal: :Soft matter 2009
Stephen A Holt Anton P Le Brun Charles F Majkrzak Duncan J McGillivray Frank Heinrich Mathias Lösche Jeremy H Lakey

To many biophysical characterisation techniques, biological membranes appear as two-dimensional structures with details of their third dimension hidden within a 5 nm profile. Probing this structure requires methods able to discriminate multiple layers a few Ångströms thick. Given sufficient resolution, neutron methods can provide the required discrimination between different biochemical compone...

Journal: :Biophysical journal 2002
Ansgar Philippsen Wonpil Im Andreas Engel Tilman Schirmer Benoit Roux Daniel J Müller

The atomic force microscope (AFM) was used to image native OmpF porin and to detect the electrostatic potential generated by the protein. To this end the OmpF porin trimers from Escherichia coli was reproducibly imaged at a lateral resolution of approximately 0.5 nm and a vertical resolution of approximately 0.1 nm at variable electrolyte concentrations of the buffer solution. At low electrolyt...

2016
Vincent Chaptal Arnaud Kilburg David Flot Benjamin Wiseman Nushin Aghajari Jean-Michel Jault Pierre Falson

This data article describes the anisotropy of diffraction observed for the centered monoclinic crystals of OmpF reported in "Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block (Chaptal et al., 2016 [1])". The datasets intensity falloff as a function of resolution are provided along with reflections along the (h,l) and (k,...

ذوالفقاری, محمدرضا, رنجبر, رضا, شکیب, پگاه, صادقی فرد, نورخدا, غفوریان, سبحان, محبی, رضا, ملکی, عباس,

مقدمه: کلبسیلاپنومونیه پاتوژن فرصت طلبی است که امروزه به عنوان یکی از مهم ترین باکتری های دخیل در عفونت های بیمارستانی است و سبب بیماری های مختلفی مانند عفونت دستگاه ادراری، سپتی سمی، پنــومونی و عفونت های داخل شکمی در بیماران بستری در بیمارستان می گردد. در این مطالعه به بررسی بیان پورین های غشای خارجی در کلبسیلاپنومونیه و ارتباط آن با آنزیم های بتالاکتاماز وسیع الطیف پرداخته شد. مواد و...

Journal: :Journal of bacteriology 1987
Y Ozawa T Mizuno S Mizushima

The roles of the first base of the Pribnow box in positive regulation of the ompC and ompF genes were studied. G- and A-to-T substitutions of the first base of the ompC and ompF Pribnow boxes, respectively, resulted in a high-level functioning of the promoters in the ompR background. The level was further enhanced significantly in the ompR+ background. The effects of other substitutions were al...

Journal: :Gene 1996
L Wang J A Huang A Phelps S Firth I H Holmes P R Reeves

Part of the porcine rotavirus outer capsid protein VP7 containing all the three antigenic regions was expressed as a chimeric protein with bacterial alkaline phosphatase (AP) in E. coli. The construct contains an ompF promoter, the DNA encoding the signal sequence and the first 12 amino acids of mature OmpF, part of vp7 and the DNA encoding mature AP. The chimeric protein is stable, retains the...

Journal: :Biochimica et Biophysica Acta (BBA) - Biomembranes 2004

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