کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8340005 1541187 2018 44 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactions
ترجمه فارسی عنوان
طیف سنجی جرم کوانتومی با مواد غیر اختصاصی برای مطالعه ساختار پروتئین و تعاملات
کلمات کلیدی
کاربنز برچسب زدن کولنال، دی اتیل پیرو کربنات، رادیکال های هیدروکسیل، طیف سنجی جرمی، ساختار پروتئین بالاتر مرتبه،
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی
Using mass spectrometry (MS) to obtain information about a higher order structure of protein requires that a protein's structural properties are encoded into the mass of that protein. Covalent labeling (CL) with reagents that can irreversibly modify solvent accessible amino acid side chains is an effective way to encode structural information into the mass of a protein, as this information can be read-out in a straightforward manner using standard MS-based proteomics techniques. The differential reactivity of proteins under two or more conditions can be used to distinguish protein topologies, conformations, and/or binding sites. CL-MS methods have been effectively used for the structural analysis of proteins and protein complexes, particularly for systems that are difficult to study by other more traditional biochemical techniques. This review provides an overview of the non-specific CL approaches that have been combined with MS with a particular emphasis on the reagents that are commonly used, including hydroxyl radicals, carbenes, and diethylpyrocarbonate. We describe the reagent and protein factors that affect the reactivity of amino acid side chains. We also include details about experimental design and workflow, data analysis, recent applications, and some future prospects of CL-MS methods.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Methods - Volume 144, 15 July 2018, Pages 79-93
نویسندگان
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