Hiyam's Journal update

Phys. Rev. Lett. 100, 087202 (2008)

17O NMR Study of the Intrinsic Magnetic Susceptibility and Spin Dynamics of the Quantum Kagome Antiferromagnet ZnCu3(OH)6Cl2
A. Olariu,1 P. Mendels,1 F. Bert,1 F. Duc,2 J. C. Trombe,2 M. A. de Vries,3 and A. Harrison3,4

We report, through 17O NMR, an unambiguous local determination of the intrinsic kagome lattice spin susceptibility as well as that created around nonmagnetic defects arising from natural Zn/Cu exchange in the S=1/2 (Cu2+) herbertsmithite ZnCu3(OH)6Cl2 compound. The issue of a singlet–triplet gap is addressed. The magnetic response around a defect is found to markedly differ from that observed in nonfrustrated antiferromagnets. Finally, we discuss our relaxation measurements in the light of Cu and Cl NMR data and suggest a flat q dependence of the excitations.




Phys. Rev. Lett. 100, 077203 (2008)

63Cu, 35Cl, and 1H NMR in the S= Kagome Lattice ZnCu3(OH)6Cl2
T. Imai,1,2 E. A. Nytko,3 B. M. Bartlett,3 M. P. Shores,3 and D. G. Nocera3

ZnCu3(OH)6Cl2 (S=) is a promising new candidate for an ideal Kagome Heisenberg antiferromagnet, because there is no magnetic phase transition down to ~50 mK. We investigated its local magnetic and lattice environments with NMR techniques. We demonstrate that the intrinsic local spin susceptibility decreases toward T=0, but that slow freezing of the lattice near ~50 K, presumably associated with OH bonds, contributes to a large increase of local spin susceptibility and its distribution. Spin dynamics near T=0 obey a power-law behavior in high magnetic fields.



J. Am. Chem. Soc., 130 (7), 2202 -2212, 2008. 10.1021/ja074244w S0002-7863(07)04244-8 Web Determination of Peptide Backbone Torsion Angles Using Double-Quantum Dipolar Recoupling Solid-State NMR Spectroscopy
Manish A. Mehta,* Matthew T. Eddy, Seth A. McNeill, Frank D. Mills, and Joanna R. Long*

Abstract:
Several approaches for utilizing dipolar recoupling solid-state NMR (ssNMR) techniques to determine local structure at high resolution in peptides and proteins have been developed. However, many of these techniques measure only one torsion angle or are accurate for only certain classes of secondary structure. Additionally, the efficiency with which these dipolar recoupling experiments suppress the deleterious effects of chemical shift anisotropy (CSA) at high magnetic field strengths varies. Dipolar recoupling with a windowless sequence (DRAWS) has proven to be an effective pulse sequence for exciting double-quantum (DQ) coherences between adjacent carbonyl carbons along the peptide backbone. By allowing this DQ coherence to evolve, it is possible to measure the relative orientations of the CSA tensors and subsequently use this information to determine the Ramachandran torsion angles and . Here, we explore the accuracies of the assumptions made in interpreting DQ-DRAWS data and demonstrate their fidelity in measuring torsion angles corresponding to a variety of secondary structures irrespective of hydrogen-bonding patterns. It is shown how a simple choice of isotopic labels and experimental conditions allows accurate measurement of backbone secondary structures without any prior knowledge. This approach is considerably more sensitive for determining structure in helices and has comparable accuracy for -sheet and extended conformations relative to other methods. We also illustrate the ability of DQ-DRAWS to distinguish between structures in heterogeneous samples.