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Finn L Aachmann

Publications and source records attributed to Finn L Aachmann.

4 recordsLinked to original sources
PubMed2006

NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase.

In the bacterium Azotobacter vinelandii, a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1-7) has been identified. These epimerases are responsible for the epimerization of beta-d-mannuronic acid to alpha-l-guluronic acid in alginate polymers. The epimerases consist of two types of structural modules, designated A (one or two copies) and R (one to seven copies). The structure of the catalytically active A-module from the smallest epimerase AlgE4 (consisting of AR) has been solved recently. This paper describes the NMR structure of the R-module from AlgE4 and its titration with a substrate analogue and paramagnetic thulium ions. The R-module folds into a right-handed parallel beta-roll. The overall shape of the R-module is an elongated molecule with a positively charged patch that interacts with the substrate. Titration of the R-module with thulium indicated possible calcium binding sites in the loops formed by the nonarepeat sequences in the N-terminal part of the molecule and the importance of calcium binding for the stability of the R-module. Structure calculations showed that calcium ions can be incorporated in these loops without structural violations and changes. Based on the structure and the electrostatic surface potential of both the A- and R-module from AlgE4, a model for the appearance of the whole protein is proposed.

Alginates↗
PubMed2005

Phase solubility and structure of the inclusion complexes of prednisolone and 6 alpha-methyl prednisolone with various cyclodextrins.

The purpose of this work was to study the inclusion binding interaction of two structurally related steroids, prednisolone and 6alpha-methyl prednisolone with a wide variety of cyclodextrins (CDs), both native (alpha-, beta- and gamma-CD) as well as modified (hydroxypropyl-, sulfobutyl ether-, glucosyl-, and maltosyl-beta-CD and sulfobutyl ether-gamma-CD), and to relate the binding constants to structural differences in the steroids. Phase-solubility diagrams of the steroids with various CDs were obtained. The stability constants (K1:1) revealed that beta-CD formed the strongest complex with prednisolone, followed by gamma-CD. With 6alpha-methyl prednisolone, the stability constants of both beta- and alpha-CD were considerably lower compared with prednisolone. In contrast, gamma-CD formed a stronger complex with 6alpha-methyl prednisolone compared with prednisolone. Derivatives of beta-CD gave slightly altered stability constants compared with native beta-CD. The structures of the complexes between the two guest molecules and native beta-CD were studied by nuclear magnetic resonance spectroscopy. This clearly showed that the introduction of the methyl group led to a different binding geometry of 6alpha-methyl prednisolone compared with prednisolone. Additionally, the nuclear magnetic resonance results indicate the presence of an additional, weaker binding site, which is less populated in prednisolone.

Cyclodextrins↗
PubMed2002

NMR diffusion as a novel tool for measuring the association constant between cyclodextrin and guest molecules.

In this paper we introduce the use of diffusion measurements by nuclear magnetic resonance (NMR) spectroscopy for determining association constants of weak and very weak interactions between cyclodextrin and guest molecules, as long as both the free and complexed guest molecules are soluble to an extent that allows good sensitivity in the NMR experiment. The experimental setup and data analysis is discussed for three different guest molecules: L-phenylalanine, L-leucine and L-valine, representing different strengths of interaction. The underlying assumptions are discussed and the scope of the method (range of K(a) values, requirements to the guest molecule) are discussed. The method's main advantage is its general applicability independent of chromogenic or electrochemical properties of the guest molecule. Whereas calorimetric methods that exhibit a similar generality, are applicable mainly to strong interactions, NMR diffusion measurements are applicable to weaker interactions down to the theoretical limit of 1 M(-1), the upper limit for K(a) values to be determined by it is approximately 200. A further advantage of the method is the low amount of sample needed. The method is in principle applicable to any case of molecular recognition between a host and guest molecule leading to weak interactions.

Calorimetry↗