The Role of Side Chains in the Fine-Tuning of the Metal-Binding Ability of Multihistidine Peptides

The systematic studies of copper(II), nickel(II) and zinc(II) ion complexes of protected multihistidine peptides containing amino acids with different side chains (Ac-SarHAH-NH₂, Ac-HADH-NH₂, Ac-HDAH-NH₂, Ac-HXHYH-NH₂ X, Y = A, F, D or K, Ac-HXHAHXH-NH₂, X = F or D) have provided information about the metal ion and protein interaction and have made it possible to draw conclusions regarding general trends in the coordination of metal complexes of multihistidine peptides. The stability of the metal complexes significantly depends on the position of the histidines and amino acids, which are present in the neighbourhood of the histidine amino acids as well. The most significant effect was observed on peptides containing aspartic acid or phenylalanine. The redox parameters of complexes, however, depend on the number and position of histidines, and the other side chain donor atoms have practically no effect on the electrochemical properties of imidazole-coordinated species. However, the presence of aspartic acid side chains results in a more distorted geometry of amide-coordinated species and increases the reducibility of these complexes.     

On minimum weight pseudo-triangulations

In this note we discuss some structural properties of minimum weight pseudo-triangulations of point sets.     

A study on thorium levels in human femur bones

The incorporation of naturally occurring thorium isotopes in human femur bones was studied by analyzing 28 bone samples. The results show that the activity concentrations of ²³²Th and ²³⁰Th are in the range of the blank values resulting in an upper limit of theirs activity concentrations in human bones. The presence of ²²⁸Th can be attributed, on the basis of model calculations, to the radioactive decay of deposited ²²⁸Ra. We conclude that thorium is not detectably incorporated into human bones.     

Sugar–Edge Interactions in a DNA–RNA G‐Quadruplex: Evidence of Sequential C−H⋅⋅⋅O Hydrogen Bonds Contributing to RNA Quadruplex Folding

DNA G‐quadruplexes were systematically modified by single riboguanosine (rG) substitutions at anti‐dG positions. Circular dichroism and NMR experiments confirmed the conservation of the native quadruplex topology for most of the DNA–RNA hybrid structures. Changes in the C8 NMR chemical shift of guanosines following rG substitution at their 3′‐side within the quadruplex core strongly suggest the presence of C8?H???O hydrogen‐bonding interactions with the O2′ position of the C2′‐endo ribonucleotide. A geometric analysis of reported high‐resolution structures indicates that such interactions are a more general feature in RNA quadruplexes and may contribute to the observed preference for parallel topologies.     

A note on the complexity of the transportation problem with a permutable demand vector

In this note we investigate the computational complexity of the transportation problem with a permutable demand vector, TP-PD for short. In the TP-PD, the goal is to permute the elements of the given integer demand vector b=(b₁,…,b_n) in order to minimize the overall transportation costs. Meusel and Burkard [6] recently proved that the TP-PD is strongly NP-hard. In their NP-hardness reduction, the used demand values b_j, j=1,…,n, are large integers. In this note we show that the TP-PD remains strongly NP-hard even for the case where b_j]{0,3} for j=1,…,n. As a positive result, we show that the TP-PD becomes strongly polynomial time solvable if b_j] {0,1,2} holds for j=1,…,n. This result can be extended to the case where b_j]{3,3+1,3+2} for an integer 3.