In pilot studies of the usefulness of solid state nuclear magnetic resonance spectroscopy in characterizing chemical and molecular structural effects of alkaptonuria on connective tissue, we have obtained (13) C spectra from articular cartilage from an AKU patient. An apparently normal anatomical location yielded a cross polarization magic angle spinning spectrum resembling literature spectra and dominated by collagen and glycosaminoglycan signals. All spectral linewidths from strongly pigmented ochronotic cartilage however were considerably increased relative to the control indicating a marked increase in collagen molecular disorder. This disordering of cartilage structural protein parallels, at the atomic level, the disordering revealed at higher length scales by microscopy. We also demonstrate that the abnormal spectra from ochronotic cartilage fit with the abnormality in the structure of collagen fibres at the ultrastructural level, whereby large ochronotic deposits appear to alter the structure of the collagen fibre by invasion and cross linking. Summary: Increased signal linewidths in solid state NMR spectra of ochronotic articular cartilage from an AKU patient relative to linewidths in normal, control, cartilage reveals a marked decrease in collagen molecular order in the diseased tissue. This atomic level disordering parallels higher length scale disorder revealed by microscopic techniques.
PMID: 21735270 [PubMed - as supplied by publisher]
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes.
J Phys Chem B. 2011 Aug 1;
Authors: Su Y, Hong M
A challenge in the application of solid-state NMR spectroscopy to membrane proteins and peptides is the relatively broad linewidths compared to solution NMR spectra. To understand the linewidth contributions to membrane protein spectra, we have measured the inhomogeneous and homogeneous...
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08-03-2011 12:00 PM
Solid-state photo-CIDNP effect observed in phototropin LOV1-C57S by (13)C magic-angle spinning NMR spectroscopy.
Solid-state photo-CIDNP effect observed in phototropin LOV1-C57S by (13)C magic-angle spinning NMR spectroscopy.
Solid-state photo-CIDNP effect observed in phototropin LOV1-C57S by (13)C magic-angle spinning NMR spectroscopy.
J Am Chem Soc. 2010 Nov 10;132(44):15542-3
Authors: Thamarath SS, Heberle J, Hore PJ, Kottke T, Matysik J
Until now, the solid-state photo-CIDNP effect, discovered in 1994 by Zysmilich and McDermott, has been observed selectively in photosynthetic systems. Here we present the first observation of this effect in a...
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03-02-2011 11:54 AM
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
J Am Chem Soc. 2010 Oct 6;132(39):13765-75
Authors: Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH
We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s...
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01-21-2011 12:00 PM
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
Magn Reson Chem. 2010 Sep;48(9):704-11
Authors: deAzevedo ER, Ayrosa AM, Faria GC, Cervantes HJ, Huster D, Bonagamba TJ, Pitombo RN, Rabbani SR
This article describes a solid-state NMR (SSNMR) investigation of the influence of hydration and chemical...
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01-21-2011 12:00 PM
[NMR paper] Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations.
Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations.
Related Articles Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations.
Biophys J. 2005 Sep;89(3):2113-20
Authors: Heise H, Luca S, de Groot BL, Grubmüller H, Baldus M
An approach is introduced to characterize conformational ensembles of intrinsically unstructured peptides on the atomic level using two-dimensional solid-state NMR data and...
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12-01-2010 06:56 PM
[NMR paper] Atomic refinement using orientational restraints from solid-state NMR.
Atomic refinement using orientational restraints from solid-state NMR.
Related Articles Atomic refinement using orientational restraints from solid-state NMR.
J Magn Reson. 2000 Nov;147(1):9-16
Authors: Bertram R, Quine JR, Chapman MS, Cross TA
We describe a procedure for using orientational restraints from solid-state NMR in the atomic refinement of molecular structures. Minimization of an energy function can be performed through either (or both) least-squares minimization or molecular dynamics employing simulated annealing. The energy, or...
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11-19-2010 08:29 PM
Protein-ice interaction of an antifreeze protein observed with solid-state NMR [Chemi
Protein-ice interaction of an antifreeze protein observed with solid-state NMR
Siemer, A. B., Huang, K.-Y., McDermott, A. E....
Date: 2010-10-12
NMR on frozen solutions is an ideal method to study fundamental questions of macromolecular hydration, because the hydration shell of many biomolecules does not freeze together with bulk solvent. In the present study, we present previously undescribed NMR methods to study the interactions of proteins with their hydration shell and the ice lattice in frozen solution. We applied these methods to compare solvent interaction of an ice-binding...
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10-13-2010 04:10 AM
Ph.D. student in solid-state NMR: Studying protein folding and assembly at atomic sca
Ph.D. student in solid-state NMR: Studying protein folding and assembly at atomic scale
Description of the Faculty / Research group
The Faculty of Science consists of six departments: Biology, Pharmaceutical Sciences, Information and Computing Sciences, Physics and Astronomy, Mathematics and Chemistry. The Faculty is home to 3500 students and nearly 2000 staff and is internationally renowned for the quality of its research.
The NMR Research Group is part of the Chemistry Department (Universiteit Utrecht fac. Scheikunde) and belongs to the Bijvoet Center for Biomolecular...