Conformational Isomerism in Monomeric,Low‐Coordinate Group 12 Complexes Stabilized by a Naphthyl‐Substituted m‐Terphenyl Ligand

The synthesis and characterization of the first series of low‐coordinate bis(terphenyl) complexes of the Group 12 metals, [Zn(2,6‐Naph₂C₆H₃)₂] ( 1 ), [Cd(OEt₂)(2,6‐Naph₂C₆H₃)₂] ( 2 ) and [Hg(OEt₂)(2,6‐Naph₂C₆H₃)₂] ( 3 ) (Naph=1‐C₁₀H₇) are described. The naphthyl substituents of the terphenyl ligands confer considerable steric bulk, and as a result of limited flexibility introduce multiple conformations to these unusual systems. In the solid state, complex 1 features a two‐coordinate Zn centre with the ligands oriented in a syn/anti conformation, whereas the three‐coordinate distorted T‐shaped complexes 2 and 3 feature the ligands in the syn/syn configurations. The results of DFT calculations are in good agreement with the solid‐state configurations for these complexes and support the spectroscopic measurements, which indicate several conformers in solution.     

MOLECULAR CONFORMATION OF IONIC SURFACTANTS IN AQUEOUS SOLUTION

The molecular conformation of ionic surfactant in aqueous solution is investigated withfluorescent probes which are intrinsic insurfactant molecules or externally introduced. Quench-lng or pyrene monomer fluorescence by alkyltriphenylphosphonium or N-alkylpyridiniumobeys Stern-Voimer equation, being diffusi6n-controlled dynamic quenching, but the behaviorof quenching with different lengths of alkyl chain is "abnormal", i.e. the longer the chain,the greater the quenching rate constant. The pyrene excimer fluorescence is observed in theaqueous solution of cetyltrimethylammonium bromide (CTMAB), and the inhibition (for cationicquenchers) and promotion (for anionic quenchers) effects of CTMAB on the quenching ofpyrene fluorescence are also observed. The self-coiling conformation of ionic surfactantmolecules in aqueous solution is proposed to be responsible for these observations and theconformation to be dynamic.     

Investigation on the conformational changes of bovine serum albumin in a wide pH range from 2 to 12

The conformation of bovine serum albumin largely depends on its microenvironment pH and affects its physical functions and applications. In this study, we investigated the effects of pH (wide range 2–12) on the conformation of bovine serum albumin based on spectroscopic signals by various spectroscopic means including fluorescence, synchronous fluorescence, resonance light scattering, UV-visible absorption, and circular dichroism. The changes in spectroscopic signals, such as peak position and intensity, showed that the structure of bovine serum albumin varied significantly with pH. The conformation of bovine serum albumin was compact at pH 6–7, as indicated by the largest peak position values and peak intensities in the fluorescence, synchronous fluorescence, and RLS spectra. The structure of bovine serum albumin became loose in the acidic or alkaline environment, as indicated by the decreased peak position values and peak intensities. The microenvironment of the amino acid residues of bovine serum albumin also varied with pH, as indicated by the changing peak position values. At pH 7, the hydrophobicity of the tyrosine and tryptophan residues was the weakest, as indicated by the minimum synchronous fluorescence signals. In addition, the secondary structure of bovine serum albumin, especially α-helix, varied with pH. The content of α-helix reached the maximum value of 68% at pH 6–8, whereas it decreased in the acidic or alkaline environment. The study provides valuable details for studying the physiological function and applications of serum albumins.     

Efficient Algorithms for Large Scale Global Optimization: Lennard-Jones Clusters

A stochastic global optimization method is applied to the challenging problem of finding the minimum energy conformation of a cluster of identical atoms interacting through the Lennard-Jones potential. The method proposed incorporates within an already existing and quite successful method, monotonic basin hopping, a two-phase local search procedure which is capable of significantly enlarging the basin of attraction of the global optimum. The experiments reported confirm the considerable advantages of this approach, in particular for all those cases which are considered in the literature as the most challenging ones, namely 75, 98, 102 atoms. While being capable of discovering all putative global optima in the range considered, the method proposed improves by more than two orders of magnitude the speed and the percentage of success in finding the global optima of clusters of 75, 98, 102 atoms.     

A thioester substrate binds to the enzyme Arthrobacter thioesterase in two ionization states: evidence from Raman difference spectroscopy

4‐Hydroxybenzoyl‐CoA (4‐HB‐CoA) thioesterase from Arthrobacter is the final enzyme catalyzing the hydrolysis of 4‐HB‐CoA to produce coenzyme A and 4‐hydroxybenzoic acid in the bacterial 4‐chlorobenzoate dehalogenation pathway. Using a mutation E73A that blocks catalysis, stable complexes of the enzyme and its substrate can be analyzed by Raman difference spectroscopy. Here we have used Raman difference spectroscopy, in the non‐resonance regime, to characterize 4‐HB‐CoA bound in the active site of the E73A thioesterase. In addition, we have characterized complexes of the wild‐type enzyme complexed with the unreactive substrate analog 4‐hydroxyphenacyl‐CoA (4‐HP‐CoA). Both sets of complexes show evidence for two forms of the ligand in the active site: one population has the 4‐hydroxy group protonated, 4‐OH; while the second has the group as the hydroxide, 4‐O⁻. For bound 4‐HP‐CoA, X‐ray data show that glutamate 78 is close to the 4‐OH in the complex and it is likely that this is the proton acceptor for the 4‐OH proton. Although the pK_a of the 4‐OH group on the free substrate in aqueous solution is 8.6, the relative populations of ionized and neutral 4‐HB‐CoA bound to E73A remain invariant between pH 7.3 and 9.8. The invariance with pH suggests that the 4‐OH and the ‐COO⁻ of E78 constitute a tightly coupled pair where their separate pK_a ‘s lose their individual qualities. Narrow band profiles are seen in the CO double bond and C‐S regions, suggesting that the hydrolyzable thioester group is rigidly bound in the active site in a syn gauche conformation. Copyright © 2011 John Wiley & Sons, Ltd.     

Microwave spectrum,centrifugal perturbation,dipole moment,and conformation of 5-methyl-1,3-dioxane

The microwave spectrum of 5-methyl-1,3-dioxane was studied in the frequency range 12–35 GHz. The a and c type rotation transitions with J≤30 were identified. The rotational constants A = 4658.5244(33) MHz, B = 2383.3930(12) MHz, and C = 1724.28907(88) MHz and the quartic constants of the centrifugal distortion of the molecule in the ground vibrational state were determined. The components of the dipole moment were found, μ _a = 1.76 ± 0.01 D and μ _c = 1.10 ± 0.01 D; the net dipole moment of the molecule is μ = 2.08 ± 0.01 D. 5-Methyl-1,3-dioxane was calculated by the B3PW91/aug-cc-pVDZ density functional theory method. The calculated data are compared with the experimental data. The most stable conformation is the chair conformation with an equatorial orientation of the methyl group.     

Study of peptide conformation in terms of the ABEEM/MM method

The ABEEM/MM model (atom-bond electronegativity equalization method fused into molecular mechanics) is applied to study of the polypeptide conformations. The Lennard-Jones and torsional parameters were optimized to be consistent with the ABEEM/MM fluctuating charge electrostatic potential. The hydrogen bond was specially treated with an electrostatic fitting function. Molecular dipole moments, dimerization energies, and hydrogen bond lengths of complexes are reasonably achieved by our model, compared to ab initio results. The ABEEM/MM fluctuating charge model reproduces both the peptide conformational energies and structures with satisfactory accuracy with low computer cost. The transferability is tested by applying the parameters of our model to the tetrapeptide of alanine and another four dipeptides. The overall RMS deviations in conformational energies and key dihedral angles for four di- or tetrapeptide, is 0.39 kcal/mol and 7.7 degrees . The current results agree well with those by the accurate ab initio method, and are comparable to those from the best existing force fields. The results make us believe that our fluctuating charge model can obtain more promising results in protein and macromolecular modeling with good accuracy but less computer cost.