[NMR paper] Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling.
Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling.
Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling.
J Am Chem Soc. 2016 Jul 14;
Authors: Salmon L, Ahlstrom LS, Horowitz S, Dickson A, Brooks CL, Bardwell JC
Abstract
Chaperones maintain a healthy proteome by preventing aggregation and by aiding in protein folding. Precisely how chaperones influence the conformational properties of their substrates, however, remains unclear. To achieve a detailed...
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07-16-2016 04:54 AM
[NMR paper] Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Related Articles Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Prog Nucl Magn Reson Spectrosc. 2015 Apr;86-87C:41-64
Authors: Burmann BM, Hiller S
Abstract
The majority of proteins depend on a well-defined three-dimensional structure to obtain their functionality. In the cellular environment, the process of protein folding is guided by molecular chaperones to avoid misfolding, aggregation, and...
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04-29-2015 03:49 PM
Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists
Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists
Publication date: April 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volumes 86–87</br>
Author(s): Björn M. Burmann , Sebastian Hiller</br>
The majority of proteins depend on a well-defined three-dimensional structure to obtain their functionality. In the cellular environment, the process of protein folding is guided by molecular chaperones to avoid misfolding, aggregation, and the generation of toxic species. To this end, living cells contain complex...
[NMR paper] Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Related Articles Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
J Biol Chem. 2013 May 3;
Authors: Esposito G, Garvey M, Alverdi V, Pettirossi F, Corazza A, Fogolari F, Polano M, Mangione PP, Giorgetti S, Stoppini M, Rekas A, Bellotti V, Heck AJ, Carver JA...
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05-07-2013 01:30 PM
[NMR paper] NMR and molecular modeling studies of the interaction between wheat germ agglutinin a
NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells.
Related Articles NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells.
Biochemistry. 2004 Aug 3;43(30):9647-54
Authors: Lycknert K, Edblad M, Imberty A, Widmalm G
The beta-D-GlcpNAc-(1-->6)-alpha-D-Manp disaccharide is a constituent of highly...
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11-24-2010 10:01 PM
[NMR paper] Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w
Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Related Articles Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Biochemistry. 2003 Sep 30;42(38):11100-8
Authors: Cai S, Stevens SY, Budor AP, Zuiderweg ER
The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic...
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[NMR paper] NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain:
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Related Articles NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Biochemistry. 1998 Jun 2;37(22):7929-40
Authors: Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER
The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision...
Capturing a Dynamic Chaperone–Substrate Interaction Using NMR-Informed Molecular Modeling
Linear Mode
