Monomer dissociation and subsequent misfolding of the transthyretin (TTR) is one of the most critical causative factors of TTR amyloidosis. TTR amyloidosis causes several human diseases, such as senile systemic amyloidosis and familial amyloid cardiomyopathy/polyneuropathy; therefore, it is important to understand the molecular details of the structural deformation and aggregation mechanisms of TTR. However, such molecular characteristics are still elusive because of the complicated structural...
Chaperonin-Based Biolayer Interferometry To Assessthe Kinetic Stability of Metastable, Aggregation-Prone Proteins
Chaperonin-Based Biolayer Interferometry To Assessthe Kinetic Stability of Metastable, Aggregation-Prone Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00293/20160819/images/medium/bi-2016-00293t_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00293
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nmrlearner
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08-19-2016 05:49 PM
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
Abstract The combination of the wide availability of protein backbone and side-chain NMR chemical shifts with advances in understanding of their relationship to protein structure makes these parameters useful for the assessment of structural-dynamic protein models. A new chemical shift predictor (PPM) is introduced, which is solely based on physicalâ??chemical contributions to the chemical shifts for both the protein backbone and methyl-bearing amino-acid side chains. To...
[NMR paper] Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-label
Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning.
Related Articles Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning.
J Biomol NMR. 2004 Apr;28(4):311-25
Authors: Fujiwara T, Todokoro Y, Yanagishita H, Tawarayama M, Kohno T, Wakamatsu K, Akutsu H
Carbon-13 and nitrogen-15 signals of fully...
nmrlearner
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11-24-2010 09:51 PM
[NMR paper] Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy an
Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation.
Related Articles Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation.
Biochemistry. 1994 Jan 11;33(1):33-41
Authors: Jarvis JA, Munro SL, Craik DJ
A peptide corresponding to the amino acid region 71-93 of the plasma protein transthyretin (TTR) has been synthesized to investigate its role in the native...
nmrlearner
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08-22-2010 03:33 AM
[NMR paper] Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy an
Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation.
Related Articles Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation.
Biochemistry. 1994 Jan 11;33(1):33-41
Authors: Jarvis JA, Munro SL, Craik DJ
A peptide corresponding to the amino acid region 71-93 of the plasma protein transthyretin (TTR) has been synthesized to investigate its role in the native...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Structural analysis of silk with 13C NMR chemical shift contour plots.
Structural analysis of silk with 13C NMR chemical shift contour plots.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural analysis of silk with 13C NMR chemical shift contour plots.
Int J Biol Macromol. 1999 Mar-Apr;24(2-3):167-71
Authors: Asakura T, Iwadate M, Demura M, Williamson MP
The polymorphic structures of silk fibroins in the solid state were examined on the basis of a quantitative relationship between the 13C chemical shift and local structure in...
nmrlearner
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08-21-2010 04:03 PM
Mapping of protein structural ensembles by chemical shifts
Abstract Applying the chemical shift prediction programs SHIFTX and SHIFTS to a data base of protein structures with known chemical shifts we show that the averaged chemical shifts predicted from the structural ensembles explain better the experimental data than the lowest energy structures. This is in agreement with the fact that proteins in solution occur in multiple conformational states in fast exchange on the chemical shift time scale. However, in contrast to the real conditions in solution at ambient temperatures, the standard NMR structural calculation methods as well chemical shift...
Aggregation-Prone Structural Ensembles of Transthyretin Collected With Regression Analysis for NMR Chemical Shift
Linear Mode
