[ASAP] Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design
Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00757/20220304/images/medium/bi1c00757_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00757
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Relationship of Sequence and Phase Separation in ProteinLow-Complexity Regions
Relationship of Sequence and Phase Separation in ProteinLow-Complexity Regions
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00008/20180316/images/medium/bi-2018-00008n_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00008
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http://feeds.feedburner.com/~r/acs/bichaw/~4/8TxFxS7r55U
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03-17-2018 12:12 PM
[NMR paper] The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
Many intrinsically disordered proteins (IDP) that fold upon binding retain conformational heterogeneity in IDP-target complexes. The thermodynamics of such fuzzy interactions is poorly understood. Here we introduce a thermodynamic framework, based on analysis of ITC and CD spectroscopy data, that provides experimental description of IDP association in terms of folding and binding contributions which can be predicted using sequence folding propensities and molecular modeling. We show how IDP can...
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09-15-2017 08:41 PM
[NMR paper] An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
Related Articles An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
Chembiochem. 2014 Feb 6;
Authors: Guan JY, Foerster JM, Drijfhout JW, Timmer M, Blok A, Ullmann GM, Ubbink M
Abstract
Protein complex formation involves an encounter state in which the proteins are associated in a nonspecific manner and often stabilized by...
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02-08-2014 05:45 PM
Sequence-Specific Mappingof the Interaction betweenUrea and Unfolded Ubiquitin from Ensemble Analysis of NMR and SmallAngle Scattering Data
Sequence-Specific Mappingof the Interaction betweenUrea and Unfolded Ubiquitin from Ensemble Analysis of NMR and SmallAngle Scattering Data
Jie-rong Huang, Frank Gabel, Malene Ringkjøbing Jensen, Stephan Grzesiek and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2118688/aop/images/medium/ja-2011-118688_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2118688
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02-23-2012 07:38 AM
[NMR paper] Automation of protein 2D proton NMR assignment by means of fuzzy mathematics and grap
Automation of protein 2D proton NMR assignment by means of fuzzy mathematics and graph theory.
Related Articles Automation of protein 2D proton NMR assignment by means of fuzzy mathematics and graph theory.
J Chem Inf Comput Sci. 1993 Sep-Oct;33(5):668-82
Authors: Xu J, Straus SK, Sanctuary BC, Trimble L
The novel methodology for protein 2D NMR assignment presented in this paper is based upon protein spin coupling graph theory analysis, fuzzy graph pattern recognition, and tree searching. The method required to formalize the whole assignment...
The sequence–ensemble relationship in fuzzy protein complexes - pnas.org
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