4.7 Article

Purifying protein complexes for mass spectrometry: applications to protein translation

期刊

METHODS
卷 35, 期 3, 页码 274-290

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2004.08.019

关键词

protein complexes; interactions; mass spectrometry; purifications; epitope tagging; affinity chromatography; translation; database searching

资金

  1. NCI NIH HHS [CA098131, T32 CA009385] Funding Source: Medline
  2. NHLBI NIH HHS [HL68744] Funding Source: Medline
  3. NIAID NIH HHS [T32 AI49824] Funding Source: Medline
  4. NIEHS NIH HHS [ES11993] Funding Source: Medline
  5. NIGMS NIH HHS [GM64779] Funding Source: Medline
  6. NINDS NIH HHS [NS43952] Funding Source: Medline

向作者/读者索取更多资源

Proteins control and mediate most of the biological activities in the cell. In most cases, proteins either interact with regulatory proteins or function in large molecular assemblies to carryout biological processes. Understanding the functions of individual proteins requires the identification of these interacting proteins. With its speed and sensitivity, mass spectrometry has become the dominant method for identifying components of protein complexes. This article reviews and discusses various approaches to purify protein complexes and analyze the proteins using mass spectrometry. As examples, methods to isolate and analyze protein complexes responsible for the translation of messenger RNAs into polypeptides are described. (c) 2004 Elsevier Inc. All rights reserved.

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