Protein Secondary Structure and Orientation in Silk as Revealed by Raman Spectromicroscopy
نویسندگان
چکیده
منابع مشابه
Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy.
Raman microspectroscopy has been used for the first time to determine quantitatively the orientation of the beta-sheets in silk monofilaments from Bombyx mori and Samia cynthia ricini silkworms, and from the spider Nephila edulis. It is shown that, for systems with uniaxial symmetry such as silk, it is possible to determine the order parameters P2 and P4 of the orientation distribution function...
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An astonishing diversity of microorganisms thrives on our planet and their activities are fundamental for the functioning of all ecosystems including the human body. Consequently, detailed insights into the functions performed by microorganisms in their natural environment are required to understand human biology and the biology of the world around us and to lay the foundations for targeted man...
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هدف از آزمایش اول بررسی اثر سطوح مختلف سریسین [0 (control), 0.1, 0.5, 1.0, 2.5 %] افزوده شده به محیط , ivm بر cumulus cell expansion، بلوغ هسته و توسعه متوالی جنین، در گوسفندان نژاد سنجابی در فصل تولید مثلی می باشد. از سرگیری میوز به وسیله خارج شدن اولین پولار بادی اندازه گیری و هم چنین درصد رسیدن جنین های دو سلولی به مرحله کلیواژ و بلاستوسیت نیز به عنوان نشانه ای از میزان شایستگی توسعه اولیه ج...
Secondary Structure and Glycosylation of Mucus Glycoproteins by Raman Spectroscopies
The major structural components of protective mucus hydrogels on mucosal surfaces are the secreted polymeric gel-forming mucins. The very high molecular weight and extensive O-glycosylation of gel-forming mucins, which are key to their viscoelastic properties, create problems when studying mucins using conventional biochemical/structural techniques. Thus, key structural information, such as the...
متن کاملThe molecular structure of spider dragline silk: folding and orientation of the protein backbone.
The design principles of spider dragline silk, nature's high-performance fiber, are still largely unknown, in particular for the noncrystalline glycine-rich domains, which form the bulk of the material. Here we apply two-dimensional solid-state NMR to determine the distribution of the backbone torsion angles (phi,psi) as well as the orientation of the polypeptide backbone toward the fiber at bo...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2007
ISSN: 0006-3495
DOI: 10.1529/biophysj.106.100339