✦ LIBER ✦

Intrinsically Disordered Protein Analysis || Localizing Flexible Regions in Proteins Using Hydrogen–Deuterium Exchange Mass Spectrometry

✍ Scribed by Uversky, Vladimir N.; Dunker, A. Keith

Book ID: 120203348
Publisher: Springer New York
Year: 2012
Weight: 556 KB
Category: Article
ISBN: 1461437040
DOI: 10.1007/978-1-4614-3704-8_25

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Hydrogen-exchange mass spectrometry for

Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins

✍ Balasubramaniam, Deepa; Komives, Elizabeth A. 📂 Article 📅 2013 🏛 Elsevier Science 🌐 English ⚖ 532 KB

Hydrogen/deuterium exchange mass spectro

Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils

✍ Alexis Nazabal; Simone Hornemann; Adriano Aguzzi; Renato Zenobi 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 552 KB

## Abstract Understanding the structural basis that distinguishes the amyloid form of the prion protein from its monomeric homologue is of crucial importance to elucidate the mechanism of the lethal diseases related to this protein. Recently, an __in vitro__ conversion system was established which

[Methods in Enzymology] Amyloid, Prions,

[Methods in Enzymology] Amyloid, Prions, and Other Protein Aggregates, Part C Volume 413 || Hydrogen/Deuterium Exchange Mass Spectrometry Analysis of Protein Aggregates

✍ Kheterpal, Indu 📂 Article 📅 2006 🏛 Elsevier 🌐 English ⚖ 418 KB