Klaus Zangger

Austria

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Articles (12)

Year:

2025

Year:

2025

The front cover artwork is provided by Markus Rotzinger at the University of Graz, Austria. The front cover picture illustrates the way the 1D exchange‐editing NMR method makes exchanging protons visible by sign alteration. The depicted spectrum of D‐glucose shows all exchanging signals inverted, thus allowing a fast qualitative determination, potentially in a single scan. Read the full text of the Research Article at 10.1002/cphc.202300713 .

Year:

2024

Year:

2024

Year:

2024

Year:

2024

Year:

2024

Year:

2023

Year:

2022

Year:

2022

Year:

AUSTRIA

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Viktoria Mueller

The James Hutton Institute

UNITED KINGDOM

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Associate Professor

Graz University of Technology

AUSTRIA

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Klaus Zangger

Research Interests

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Articles (12)

A Single-Domain VNAR Nanobody Binds with High-Affinity and Selectivity to the Heparin Pentasaccharide Fondaparinux

Quantification of Hydrogen Peroxide in PVP and PVPVA Using 1H qNMR Spectroscopy

Identifying Exchangeable Protons in a 1D NMR Spectrum by Spatially Selective Exchange‐Editing

A multi-platform approach for the comprehensive analysis of per- and polyfluoroalkyl substances (PFAS) and fluorine mass balance in commercial ski wax products

Investigation of the Influence of Copovidone Properties and Hot-Melt Extrusion Process on Level of Impurities, In Vitro Release, and Stability of an Amorphous Solid Dispersion Product

Front Cover: Identifying Exchangeable Protons in a 1D NMR Spectrum by Spatially Selective Exchange‐Editing (ChemPhysChem 8/2024)

Identifying Exchangeable Protons in a 1D NMR Spectrum by Spatially Selective Exchange‐Editing

High-Performance Thermoplastics from a Unique Bicyclic Lignin-Derived Diol

An all-at-once 2D CEST by F1-spatial frequency encoding

Overexpression of recombinant proteins containing non-canonical amino acids in Vibrio natriegens: p-azido-L-phenylalanine as coupling site for 19F-tags

Phase Behavior of Drug–Lipid–Surfactant Ternary Systems toward Understanding the Annealing-Induced Change

The periplasmic domains of Vibriocholerae ToxR and ToxS are forming a strong heterodimeric complex independent on the redox state of ToxR cysteines

Collaborators (10)

David Clases

Gregor Trimmel

Dr. Varun Kushwah

Joerg Feldmann

Nina Gubensäk

Viktoria Mueller

Katalin Barta

Dmytro Neshchadin

Joachim Reidl

Amrit Paudel

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