You have full text access to this Open Access content

ChemistryOpen

Articles are published under the terms of the Creative Commons License as stated in the final article.

Cover image for Vol. 4 Issue 6

Editors: Karen Hindson, Haymo Ross; Deputy Editor: Natalia Ortúzar

Impact Factor: 3.25

ISI Journal Citation Reports © Ranking: 2014: 40/157 (Chemistry Multidisciplinary)

Online ISSN: 2191-1363

Associated Title(s): Angewandte Chemie International Edition, Chemistry - A European Journal, Chemistry – An Asian Journal

Virtual Issue

Structure Characterization of Biomolecules

This virtual issue features articles with focus on the structural characterization of biomolecules, among them proteins, deoxyribonucleic (DNA) and ribonucleic (RNA) acids, and synthetic antibiotic derivatives designed for specific interaction with DNA.

Common to all studies here is the use of newly developed or refined experimental approaches for obtaining deeper insight into biomolecular folding and binding. Specific aspects addressed include the dynamics of biomolecular structure, weak and transient binding, aggregation, structural preorganization, and intrinsically disordered proteins.

Taken together, the articles in this virtual issue beautifully highlight the fruitful interplay between sophisticated chemical synthesis, top-notch solution measurements, and nifty gas phase techniques for the characterization of biomolecular structure, binding, and dynamics.

Articles

Kathrin Breuker
Structure Characterization of Biomolecules [Editorial]

Structure Characterization of BiomoleculesInsight into structural diversity! The articles of this virtual issue focus on the structural characterization of biomolecules. Common to all included studies is the use of newly developed or refined experimental approaches for obtaining deeper insight into biomolecular folding and binding.

ChemistryOpen 2014, 3, 137

Gleb G. Mironov, Victor Okhonin, Nasrin Khan, Christopher M. Clouthier, Maxim V. Berezovski
Conformational Dynamics of DNA G-Quadruplex in Solution Studied by Kinetic Capillary Electrophoresis Coupled On-line with Mass Spectrometry [Cover Profile]

Conformational Dynamics of DNA G-Quadruplex in Solution Studied by Kinetic Capillary Electrophoresis Coupled On-line with Mass SpectrometryWe did not expect such a big difference in migration time between folded and unfolded DNA. Our initial guess was that we could measure only a thermodynamic folding constant, but not rate constants for the fast conformational change.”

ChemistryOpen 2014, 3, 38

Gleb G. Mironov, Victor Okhonin, Nasrin Khan, Christopher M. Clouthier, Maxim V. Berezovski
Conformational Dynamics of DNA G-Quadruplex in Solution Studied by Kinetic Capillary Electrophoresis Coupled On-line with Mass Spectrometry [Full Paper]

Conformational Dynamics of DNA G-Quadruplex in Solution Studied by Kinetic Capillary Electrophoresis Coupled On-line with Mass Spectrometry Combining forces! Kinetic capillary electrophoresis is coupled on-line with mass spectrometry (KCE-MS) to study conformational dynamics of DNA G-quadruplexes in solution. Peak's shift and its widening in KCE help measure rate and equilibrium constants; and ion mobility spectrometry (IMS) provides relative sizes, absolute molecular masses and stoichiometry.

ChemistryOpen 2014, 3, 58–64

Ursula M. Kotyrba, Kevin Pröpper, Eike-F. Sachs, Anastasiya Myanovska, Tobias Joppe, Friederike Lissy, George M. Sheldrick, Konrad Koszinowski1 and Ulf Diederichsen
Triostin A Derived Cyclopeptide as Architectural Template for the Alignment of Four Recognition Units [Full Paper]

Triostin A Derived Cyclopeptide as Architectural Template for the Alignment of Four Recognition UnitsDesigned to match! Four nucleobases were attached to the disulfide bridged cyclopeptide scaffold derived from the DNA bisintercalator triostin. The aza-TANDEM backbone provides organization and alignment of the nucleobases, allowing for application in sequence-dependent DNA recognition and molecular architecture.

ChemistryOpen 2014, 3, 152–160

Tomáš Sára, Thomas C. Schwarz, Dennis Kurzbach, Christoph H. Wunderlich, Christoph Kreutz, Robert Konrat
Magnetic Resonance Access to Transiently Formed Protein Complexes [Full Paper]]

Magnetic Resonance Access to Transiently Formed Protein ComplexesObserving the unobserved: Low-affinity protein–protein complexes of transiently interacting proteins are hallmarks of signaling cascades and of great relevance in biology. We show how novel NMR and EPR techniques can be used for characterizing weak protein–protein complexes and their potential to study hitherto unobserved higher-order structures of proteins.

ChemistryOpen 2014, 3, 115–123

Nicholas Zinck, Ann-Kathrin Stark, Derek J. Wilson, and Michal Sharon
An Improved Rapid Mixing Device for Time-Resolved Electrospray Mass Spectrometry Measurements

An Improved Rapid Mixing Device for Time-Resolved Electrospray Mass Spectrometry MeasurementsIn the flow! The development of an improved continuous-flow mixing apparatus for real-time electrospray mass spectrometry measurements is described. The performance of the device is demonstrated by monitoring the unfolding reaction of cytochrome C, yielding improved signal-to-noise ratio and reduced experimental repeat errors.

ChemistryOpen 2014, 3, 109–114

SEARCH

SEARCH BY CITATION