On NMR isotropic chemical shift surfaces of peptide models
نویسندگان
چکیده
منابع مشابه
Ab Initio Calculation 29Si NMR Chemical Shift Studies on Silicate Species in Aqueous and Gas Phase
Nowadays NMR spectroscopy becomes a powerful tool in chemistry because of the NMR chemical shifts. Hartree–Fock theory and the Gauge-including atomic orbital (GIAO) methods are used in the calculation of 29Si NMR chemical shifts of various silicate species in the silicate solution as initial components for zeolite synthesis both in gas and solution phase. Calculations have been performed at geo...
متن کاملBioinformatics Methods for NMR Chemical Shift Data
Nuclear magnetic resonance spectroscopy (NMR) is one of the most important methods for measuring the three-dimensional structure of biomolecules. Despite major progress in the NMR methodology, the solution of a protein structure is still a tedious and time-consuming task. The goal of this thesis is to develop bioinformatics methods which may strongly accelerate the NMR process. This work concen...
متن کاملEnergy landscapes of a hairpin peptide including NMR chemical shift restraints.
Methods recently introduced to improve the efficiency of protein structure prediction simulations by adding a restraint potential to a molecular mechanics force field introduce additional input parameters that can affect the performance. Here we investigate the changes in the energy landscape as the relative weight of the two contributions, force field and restraint potential, is systematically...
متن کاملAn NMR Crystallographic Investigation of the Relationships between the Crystal Structure and 29Si Isotropic Chemical Shift in Silica Zeolites
NMR crystallography has recently been applied to great effect for silica zeolites. Here we investigate whether it is possible to extend the structural information available from routine NMR spectra via a simple structure-spectrum relationship. Unlike previous empirically derived relationships that have compared experimental crystal structures for (often disordered) silicates with experimental N...
متن کاملC(alpha) chemical shift tensors in helical peptides by dipolar-modulated chemical shift recoupling NMR.
The C(alpha) chemical shift tensors of proteins contain information on the backbone conformation. We have determined the magnitude and orientation of the C(alpha) chemical shift tensors of two peptides with a-helical torsion angles: the Ala residue in G*AL (phi = -65.7 degrees, psi = -40 degrees), and the Val residue in GG*V (phi = -81.5 degrees, psi = -50.7 degrees). The magnitude of the tenso...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Molecular Structure: THEOCHEM
سال: 2004
ISSN: 0166-1280
DOI: 10.1016/j.theochem.2003.12.034