CSI-LSTM: a web server to predict protein secondary structure using bidirectional long short term memory and NMR chemical shifts
CSI-LSTM: a web server to predict protein secondary structure using bidirectional long short term memory and NMR chemical shifts
Abstract
Protein secondary structure provides rich structural information, hence the description and understanding of protein structure relies heavily on it. Identification or prediction of secondary structures therefore plays an important role in protein research. In protein NMR studies, it is more convenient to predict secondary structures from chemical shifts as compared to the traditional determination methods based on...
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09-14-2021 12:38 AM
[NMR paper] CSI-LSTM: a web server to predict protein secondary structure using bidirectional long short term memory and NMR chemical shifts
CSI-LSTM: a web server to predict protein secondary structure using bidirectional long short term memory and NMR chemical shifts
Protein secondary structure provides rich structural information, hence the description and understanding of protein structure relies heavily on it. Identification or prediction of secondary structures therefore plays an important role in protein research. In protein NMR studies, it is more convenient to predict secondary structures from chemical shifts as compared to the traditional determination methods based on inter-nuclear distances provided by NOESY...
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09-14-2021 12:38 AM
[NMR paper] Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR.
Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.frontiersin.org-alerts-logo-Logo_LinkOut.jpg http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR.
Front Mol Biosci. 2020;7:17
Authors: Wiegand T, Lacabanne D, Torosyan A, Boudet J, Cadalbert R, Allain FH, Meier BH,...
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03-16-2020 04:59 PM
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
From The DNP-NMR Blog:
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
Sarkar, R., et al., Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity. Solid State Nucl Magn Reson, 2016. 76-77: p. 7-14.
http://www.ncbi.nlm.nih.gov/pubmed/27017576
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07-22-2016 02:21 PM
[NMR paper] Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity.
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity.
Related Articles Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity.
Solid State Nucl Magn Reson. 2016 Mar 15;76-77:7-14
Authors: Sarkar R, Mainz A, Busi B, Barbet-Massin E, Kranz M, Hofmann T, Reif B
Abstract
In recent years, MAS solid-state NMR has emerged as a technique for the investigation of soluble protein complexes. It was found that high molecular weight complexes do not need...
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03-29-2016 01:43 AM
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
Publication date: Available online 15 March 2016
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Riddhiman Sarkar, Andi Mainz, Baptiste Busi, Emeline Barbet-Massin, Maximilian Kranz, Thomas Hofmann, Bernd Reif</br>
In recent years, MAS solid-state NMR has emerged as a technique for the investigation of soluble protein complexes. It was found that high molecular weight complexes do not need to be crystallized in order to obtain an immobilized...
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03-16-2016 12:13 AM
Improving protein solubility & long-term stability
Has anybody successfully used the following method?
A simple method for improving protein solubility and long-term stability.
Golovanov AP, Hautbergue GM, Wilson SA, Lian LY.
Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, P. O. Box 88, Manchester M60 1QD, UK. a.golovanov@umist.ac.jp
J Am Chem Soc. 2004 Jul 28;126(29):8933-9.
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Proteins
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01-22-2014 07:04 PM
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
J Phys Chem B. 2011 Feb 10;
Authors: Bertelsen K, Vad B, Nielsen EH, Hansen SK, Skrydstrup T, Otzen DE, Vosegaard T, Nielsen NC
Recently, ether lipids have been introduced as long-term stable alternatives to the more natural,...