کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8340489 1541237 2015 13 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Probing structures of large protein complexes using zero-length cross-linking
ترجمه فارسی عنوان
ساختار پروتئین های پروتئین های بزرگ با استفاده از اتصال متقابل صفر
کلمات کلیدی
طیف سنجی جرمی، ساختار، پیوند شیمیایی، صفر طول متقابل، شناسایی صلیب لینک، مدلسازی مولکولی،
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی
Structural mass spectrometry (MS) is a field with growing applicability for addressing complex biophysical questions regarding proteins and protein complexes. One of the major structural MS approaches involves the use of chemical cross-linking coupled with MS analysis (CX-MS) to identify proximal sites within macromolecules. Identified cross-linked sites can be used to probe novel protein-protein interactions or the derived distance constraints can be used to verify and refine molecular models. This review focuses on recent advances of “zero-length” cross-linking. Zero-length cross-linking reagents do not add any atoms to the cross-linked species due to the lack of a spacer arm. This provides a major advantage in the form of providing more precise distance constraints as the cross-linkable groups must be within salt bridge distances in order to react. However, identification of cross-linked peptides using these reagents presents unique challenges. We discuss recent efforts by our group to minimize these challenges by using multiple cycles of LC-MS/MS analysis and software specifically developed and optimized for identification of zero-length cross-linked peptides. Representative data utilizing our current protocol are presented and discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Methods - Volume 89, 1 November 2015, Pages 99-111
نویسندگان
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