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Ralf W. Glaser

Researcher at University of Jena

Publications -  34
Citations -  2456

Ralf W. Glaser is an academic researcher from University of Jena. The author has contributed to research in topics: Epitope & Fluorine-19 NMR. The author has an hindex of 19, co-authored 34 publications receiving 2370 citations. Previous affiliations of Ralf W. Glaser include Schiller International University & ETH Zurich.

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Journal ArticleDOI

Reversible electrical breakdown of lipid bilayers: formation and evolution of pores.

Ralf W. Glaser, +4 more
- 24 May 1988 - 
TL;DR: The mechanism of reversible electric breakdown of lipid membranes is studied and hydrophilic pores of an effective radius of 0.6 up to more than 1 nm are formed, which account for the membrane conductivity increase observed.
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Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism.

Uwe Sauer, +7 more
- 01 Nov 1999 - 
TL;DR: Data indicate remarkable robustness and rigidity in central carbon metabolism in the presence of genetic variation and more significant physiological changes and flux ratio differences were seen in response to altered environmental conditions.
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Antigen-Antibody Binding and Mass Transport by Convection and Diffusion to a Surface: A Two-Dimensional Computer Model of Binding and Dissociation Kinetics

Ralf W. Glaser
- 15 Aug 1993 - 
TL;DR: The kinetics of binding and dissociation between a soluble analyte and an immobilized ligand on or near a surface are described numerically by an iterative computer model applied to a microflow chamber used for surface plasmon resonance measurements.
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Concentration-Dependent Realignment of the Antimicrobial Peptide PGLa in Lipid Membranes Observed by Solid-State 19F-NMR

Ralf W. Glaser, +6 more
- 01 May 2005 - 
TL;DR: The membrane-disruptive antimicrobial peptide PGLa is found to change its orientation in a dimyristoyl-phosphatidylcholine bilayer when its concentration is increased to biologically active levels.
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4‐Fluorophenylglycine as a Label for 19F NMR Structure Analysis of Membrane‐Associated Peptides

Sergii Afonin, +7 more
- 07 Nov 2003 - 
TL;DR: The non‐natural amino acid 4‐fluorophenylglycine (4F‐Phg) was incorporated into several representative membrane‐associated peptides for dual purpose and its fusion activities suggest that the peptide is less structured in the fusogenic transition state than in the helical ground state.