𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Analysis of post-translational modification and characterization of the domain structure of dynamin A from Dictyostelium discoideum

✍ Scribed by Andreas Schlosser; Boris Klockow; Dietmar J. Manstein; Wolf D. Lehmann

Publisher
John Wiley and Sons
Year
2003
Tongue
English
Weight
284 KB
Volume
38
Category
Article
ISSN
1076-5174

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

The post‐translational modifications of the 96 kDa protein dynamin A from Dictyostelium discoideum were analyzed using Q‐TOF mass spectrometry. The accurate molecular mass of the intact protein revealed a covalent modification causing an additional mass of 42 Da. The modification could be identified as N‐terminal acetylation by tandem mass spectrometry. Extracted ion chromatograms for the a~1~ and b~1~ ion of the tryptic T1 peptide were used to detect the acetylated peptide within 54 nanoelectrospray ionization tandem mass spectra. Owing to the accurate molecular mass of the intact protein, additional covalent modifications could be excluded. In addition to the covalent modification, the domain structure of dynamin A was determined by applying a combination of limited proteolysis, sodium dodecylsulfate polyacrylamide gel electrophoresis, automated tandem mass spectrometry and protein database searching. Copyright © 2003 John Wiley & Sons, Ltd.

📜 SIMILAR VOLUMES

Structural heterogeneity, post-translati
Structural heterogeneity, post-translational modifications, and biological activities of SV-IV, a major protein secreted from the rat seminal vesicle epithelium
✍ Pasquale Ferranti; Gianfranco Mamone; Antonio Malorni; John Guardiola; Paola Sti 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 224 KB 👁 2 views

The primary structure of purified SV-IV, a major secretory protein synthesized by the rat seminal vesicle (SV) epithelium, was analysed by electrospray mass spectrometry (ES-MS). The protein was found to be highly heterogeneous. The various components were separated and identified by reversed phase

Structural characterization of the N-ter
Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24
✍ Brandon A. Wustman; Daniel E. Morse; John Spencer Evans 📂 Article 📅 2004 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 218 KB 👁 1 views

## Abstract The AP7 and AP24 proteins represent a class of mineral‐interaction polypeptides that are found in the aragonite‐containing nacre layer of mollusk shell (__H. rufescens__). These proteins have been shown to preferentially interfere with calcium carbonate mineral growth in vitro. It is be

Structural characterization of a procyan
Structural characterization of a procyanidin tetramer and pentamer from the apple by low-temperature NMR analysis
✍ Yutaka Abe; Toshihiko Shoji; Nobuo Kawahara; Hiroyuki Kamakura; Tomomasa Kanda; 📂 Article 📅 2008 🏛 Elsevier Science 🌐 French ⚖ 969 KB

The structures of a procyanidin tetramer and pentamer from unripe apple (Malus pumila) were elucidated by low-temperature NMR analysis at À34 °C. These structures were [epicatechin-(4b?6)-epicatechin-(4b?8)-epicatechin-(4b?8)-epicatechin (1)] and [epicatechin-(4b?8)-epicatechin-(4b?8)-epicatechin-(4

Synthesis and Crystal Structure Determin
Synthesis and Crystal Structure Determinations in the Γ and δ Phase Domains of the Iron–Zinc System: Electronic and Bonding Analysis of Fe13Zn39 and FeZn10, a Subtle Deviation from the Hume–Rothery Standard?
✍ Claude H.E. Belin; Renaud C.H. Belin 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 581 KB

The iron+zinc system has been investigated in the zinc-rich domain. Alloying of Fe and Zn in ZnCl 2 6ux allowed the formation of well-developed single crystals of phases Fe 13 Zn 39 and FeZn 10 in a one-step experiment. These phases crystallize in cubic space group I4 3m ( ) phase, Fe 13 Zn 39 , a ‫