𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Characterization of intermolecular β-sheet peptides by mass spectrometry and hydrogen isotope exchange

✍ Scribed by Mario Kraus; Katharina Janek; Michael Bienert; Eberhard Krause

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
193 KB
Volume
14
Category
Article
ISSN
0951-4198

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Characterization of Aspartic Acid and β-
Characterization of Aspartic Acid and β-Aspartic Acid in Peptides by Fast-atom Bombardment Mass Spectrometry and Tandem Mass Spectrometry
✍ S. Castet; C. Enjalbal; P. Fulcrand; J. F. Guichou; J. Martinez; J. -L. Aubagnac 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 316 KB 👁 1 views

In this paper, we have shown that it is possible to differentiate an aspartic acid residue from its p-aspartic acid isomer in dipeptides according to the characteristic fragmentation pathways, i.e. specific immonium ion formation and cleavages involving side-chain atoms.

Unfolding dynamics of aβ-sheet protein s
Unfolding dynamics of aβ-sheet protein studied by mass spectrometry
✍ Eyles, Stephen J.; Dresch, Thomas; Gierasch, Lila M.; Kaltashov, Igor A. 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 174 KB 👁 1 views

The unfolding dynamics of cellular retinoic acid-binding protein I (CRABP I), an 18 kDa predominantly b-sheet protein, were studied by monitoring the hydrogen-deuterium (H-D) exchange reaction under various solution conditions. A bimodal charge state distribution was observed when a denaturing agent

Identification of non-covalent structure
Identification of non-covalent structure in apocytochromec by hydrogen exchange and mass spectrometry
✍ Raza, Ashraf S.; Dharmasiri, Kuruppu; Smith, David L. 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 96 KB 👁 1 views

Apocytochrome c, the in vivo precursor to active cytochrome c, was analyzed by amide hydrogen exchange and mass spectrometry to search for fixed, non-covalent structure. The protein was incubated in H 2 O at pH 3.3 or 6.7 for various times, then exposed to D 2 O to initiate isotope labeling of unfol

Probing the Non-covalent Structure of Pr
Probing the Non-covalent Structure of Proteins by Amide Hydrogen Exchange and Mass Spectrometry
✍ Smith, David L.; Deng, Yuzhong; Zhang, Zhongqi 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 403 KB 👁 1 views

The rates at which hydrogens located at peptide amide linkages in proteins undergo isotopic exchange when a protein is exposed to depend on whether these amide hydrogens are hydrogen bonded and whether they are D 2 O accessible to the aqueous solvent. Hence, amide hydrogen exchange rates are a sensi

Characterization of Hydrogen-Bonded Supr
Characterization of Hydrogen-Bonded Supramolecular Assemblies by MALDI-TOF Mass Spectrometry after Ag+ Labeling
✍ Katrina A. Jolliffe; Mercedes Crego Calama; Roel Fokkens; Nico M. M. Nibbering; 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 166 KB 👁 1 views

Synthesis based on the formation of noncovalent bonds provides a valuable alternative to the classical chemistry of covalent bonds. It has developed into an area of enormous interest for a wide variety of scientific and technological disciplines, ranging from materials science to molecular electroni