2C1400 Structure of the L- and R-type straight flagellar filament from Salmonella by electron cryomicroscopy
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چکیده
منابع مشابه
Structure and Intermolecular Interactions between L-Type Straight Flagellar Filaments.
Bacterial mobility is powered by rotation of helical flagellar filaments driven by rotary motors. Flagellin isolated from the Salmonella Typhimurium SJW1660 strain, which differs by a point mutation from the wild-type strain, assembles into straight filaments in which flagellin monomers are arranged in a left-handed helix. Using small-angle x-ray scattering and osmotic stress methods, we invest...
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Voltage-dependent L-type Ca(2+) channels play important functional roles in many excitable cells. We present a three-dimensional structure of an L-type Ca(2+) channel. Electron cryomicroscopy in conjunction with single-particle processing was used to determine a 30-A resolution structure of the channel protein. The asymmetrical channel structure consists of two major regions: a heart-shaped reg...
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چکیده ندارد.
the underlying structure of language proficiency and the proficiency level
هدف از انجام این تخقیق بررسی رابطه احتمالی بین سطح مهارت زبان خارجی (foreign language proficiency) و ساختار مهارت زبان خارجی بود. تعداد 314 زبان آموز مونث و مذکر که عمدتا دانشجویان رشته های زبان انگلیسی در سطوح کارشناسی و کارشناسی ارشد بودند در این تحقیق شرکت کردند. از لحاظ سطح مهارت زبان خارجی شرکت کنندگان بسیار با هم متفاوت بودند، (75 نفر سطح پیشرفته، 113 نفر سطح متوسط، 126 سطح مقدماتی). کلا ...
15 صفحه اولStructure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy
The large (L) proteins of non-segmented, negative-strand RNA viruses, a group that includes Ebola and rabies viruses, catalyze RNA-dependent RNA polymerization with viral ribonucleoprotein as template, a non-canonical sequence of capping and methylation reactions, and polyadenylation of viral messages. We have determined by electron cryomicroscopy the structure of the vesicular stomatitis virus...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2002
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.42.s104_2