[NMR paper] Quantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry.
Related ArticlesQuantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry.
Biochim Biophys Acta. 2015 Jan 12;
Authors: Papaioannou A, Louis M, Dhital B, Ho HP, Chang EJ, Boutis GS
Abstract
Methods for isolating elastin from fat, collagen, and muscle, commonly used in the design of artificial elastin based biomaterials, rely on exposing tissue to harsh pH levels and temperatures that usually denature many proteins. At present, a quantitative measurement of the modifications to elastin following isolation from other extracellular matrix constituents has not been reported. Using magic angle spinning (13)C NMR spectroscopy and relaxation methodologies, we have measured the modification in structure and dynamics following three known purification protocols. Our experimental data reveal that the (13)C spectra of the hydrated samples appear remarkably similar across the various purification methods. Subtle differences in the half maximum widths were observed in the backbone carbonyl suggesting possible structural heterogeneity across the different methods of purification. Additionally, small differences in the relative signal intensities were observed between purified samples. Lyophilizing the samples results in a reduction of backbone motion and reveals additional differences across the purification methods studied. These differences were most notable in the alanine motifs indicating possible changes in cross-linking or structural rigidity. The measured correlation times of glycine and proline moieties are observed to also vary considerably across the different purification methods, which may be related to peptide bond cleavage. Lastly, the relative concentration of desmosine cross-links in the samples quantified by MALDI mass spectrometry is reported.
PMID: 25592991 [PubMed - as supplied by publisher]
[NMR paper] Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Chem Commun (Camb). 2013 Feb 26;
Authors: Takaoka Y, Kioi Y, Morito A, Otani J, Arita K, Ashihara E, Ariyoshi M, Tochio H, Shirakawa M, Hamachi I
Abstract
Here we describe how a (19)F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with...
nmrlearner
Journal club
0
02-27-2013 06:47 PM
Quantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemes
Quantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemes
Abstract Nitrogen-15 Carr-Purcell-Meiboom-Gill (CPMG) transverse relaxation experiment are widely used to characterize protein backbone dynamics and chemical exchange parameters. Although an accurate value of the transverse relaxation rate, R2, is needed for accurate characterization of dynamics, the uncertainty in the R2 value depends on the experimental settings and the details of the data analysis itself. Here, we present an analysis of the impact of CPMG pulse phase...
nmrlearner
Journal club
0
04-03-2012 07:56 AM
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Chem Commun (Camb). 2010 Sep 28;46(36):6714-6
Authors: Jenkins JE, Creager MS, Butler EB, Lewis RV, Yarger JL, Holland GP
Two-dimensional homo- and heteronuclear solid-state MAS NMR experiments on (13)C/(15)N-proline labeled Argiope aurantia dragline silk provide evidence for an elastin-like beta-turn structure for the repetitive Gly-Pro-Gly-X-X motif prevalent in major...
nmrlearner
Journal club
0
12-28-2010 03:31 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...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Related Articles Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Magn Reson Chem. 2004 Feb;42(2):267-75
Authors: Yao XL, Conticello VP, Hong M
Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic...
nmrlearner
Journal club
0
11-24-2010 09:25 PM
[NMR paper] Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysi
Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Related Articles Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Biopolymers. 2003 Oct;70(2):158-68
Authors: Hong M, Isailovic D, McMillan RA, Conticello VP
The conformation of an elastin-mimetic recombinant protein, 39, is investigated using solid-state NMR spectroscopy. The protein is extensively labeled with 13C and 15N, and two-dimensional 13C-13C and 15N-13C correlation experiments were carried out to resolve and...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Related Articles Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Biophys J. 2002 Feb;82(2):1086-95
Authors: Perry A, Stypa MP, Tenn BK, Kumashiro KK
Elastin is the principal protein component of the elastic fiber in vertebrate tissue. The waters of hydration in the elastic fiber are believed to play a critical role in the structure and function of this largely hydrophobic, amorphous protein. (13)C CPMAS NMR spectra are acquired for...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Lipid analysis of human HDL and LDL by MALDI-TOF mass spectrometry and (31)P-NMR.
Lipid analysis of human HDL and LDL by MALDI-TOF mass spectrometry and (31)P-NMR.
Related Articles Lipid analysis of human HDL and LDL by MALDI-TOF mass spectrometry and (31)P-NMR.
J Lipid Res. 2001 Sep;42(9):1501-8
Authors: Schiller J, Zschörnig O, Petkovi? M, Müller M, Arnhold J, Arnold K
The analysis of HDL and LDL is important for the further understanding of atherosclerosis because changes of the protein and lipid moieties occur under pathological conditions. Because destruction of lipids leads to the formation of well-defined products...
Quantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry.
Linear Mode
