Protein Structural Analysis via Mass Spectrometry-Based Proteomics.
Adv Exp Med Biol
; 919: 397-431, 2016.
Article
em En
| MEDLINE
| ID: mdl-27975228
ABSTRACT
Modern mass spectrometry (MS) technologies have provided a versatile platform that can be combined with a large number of techniques to analyze protein structure and dynamics. These techniques include the three detailed in this chapter (1) hydrogen/deuterium exchange (HDX), (2) limited proteolysis, and (3) chemical crosslinking (CX). HDX relies on the change in mass of a protein upon its dilution into deuterated buffer, which results in varied deuterium content within its backbone amides. Structural information on surface exposed, flexible or disordered linker regions of proteins can be achieved through limited proteolysis, using a variety of proteases and only small extents of digestion. CX refers to the covalent coupling of distinct chemical species and has been used to analyze the structure, function and interactions of proteins by identifying crosslinking sites that are formed by small multi-functional reagents, termed crosslinkers. Each of these MS applications is capable of revealing structural information for proteins when used either with or without other typical high resolution techniques, including NMR and X-ray crystallography.
Palavras-chave
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Espectrometria de Massas
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Proteínas
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Biologia Computacional
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Proteoma
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Bases de Dados de Proteínas
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Proteômica
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Mineração de Dados
Tipo de estudo:
Prognostic_studies
Limite:
Animals
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Humans
Idioma:
En
Revista:
Adv Exp Med Biol
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Estados Unidos