[NMR paper] Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy
Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy
The folding of many proteins can begin during biosynthesis on the ribosome and can be modulated by the ribosome itself. Such perturbations are generally believed to be mediated through interactions between the nascent chain and the ribosome surface, but despite recent progress in characterising interactions of unfolded states with the ribosome, and their impact on the initiation of co-translational folding, a complete quantitative analysis of interactions across both...
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[ASAP] Capturing Membrane Protein Ribosome Nascent Chain Complexes in a Native-like Environment for Co-translational Studies
Capturing Membrane Protein Ribosome Nascent Chain Complexes in a Native-like Environment for Co-translational Studies
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00423/20200724/images/medium/bi0c00423_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00423
http://feeds.feedburner.com/~r/acs/bichaw/~4/WFH3x3vJplk
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[NMR paper] A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
Related Articles A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
Nat Protoc. 2016 Aug;11(8):1492-1507
Authors: Cassaignau AM, Launay HM, Karyadi ME, Wang X, Waudby CA, Deckert A, Robertson AL, Christodoulou J, Cabrita LD
Abstract
During biosynthesis on the ribosome, an elongating nascent polypeptide chain can begin to fold, in a process that is central...
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[NMR paper] Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
Related Articles Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
J Biomol NMR. 2015 Aug 8;
Authors: Chan SH, Waudby CA, Cassaignau AM, Cabrita LD, Christodoulou J
Abstract
The translational diffusion of macromolecules can be examined non-invasively by...
[NMR paper] Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of
Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol.
J Mol Biol. 1996 Apr 5;257(3):669-83
Authors: Buck M, Schwalbe H, Dobson CM
15N NMR relaxation measurements have been used to study the dynamic...
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[NMR paper] Internal mobility in the partially folded DNA binding and dimerization domains of GAL
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
Biochemistry. 1996 Feb 27;35(8):2674-86
Authors: Lefevre JF, Dayie KT, Peng JW, Wagner G
The DNA binding domain (residues 1--65) of the yeast transcriptional...
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[NMR paper] NMR characterization of partially folded and unfolded conformational ensembles of pro
NMR characterization of partially folded and unfolded conformational ensembles of proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR characterization of partially folded and unfolded conformational ensembles of proteins.
Biopolymers. 1999;51(3):191-207
Authors: Barbar E
Studies of unfolded and partially folded proteins provide important insight into the initiation and process of protein folding. This review focuses on the...
The ribosome stabilizes partially folded intermediates of a nascent multi-domain protein - Nature.com
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