[ASAP] Reframing the Protein Folding Problem: Entropy as Organizer
Reframing the Protein Folding Problem: Entropy as Organizer
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00687/20211202/images/medium/bi1c00687_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00687
More...
nmrlearner
Journal club
0
12-03-2021 05:33 PM
[ASAP] Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00552/20180703/images/medium/bi-2018-005525_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00552
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/QJjXPpa0z9I
More...
nmrlearner
Journal club
0
07-06-2018 09:40 AM
[ASAP] Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00552/20180703/images/medium/bi-2018-005525_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00552
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/QJjXPpa0z9I
More...
nmrlearner
Journal club
0
07-06-2018 09:40 AM
[ASAP] Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR
Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR
Cyril Charlier, Joseph M. Courtney, T. Reid Alderson, Philip Anfinrud, Ad Bax
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b04833/20180625/images/medium/ja-2018-04833s_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b04833
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Wf5C6etrn-c
nmrlearner
Journal club
0
06-25-2018 11:22 PM
Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR
Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR
Abstract
The study of intermediates in the protein folding pathway provides a wealth of information about the energy landscape. The intermediates also frequently initiate pathogenic fibril formations. While observing the intermediates is difficult due to their transient nature, extreme conditions can partially unfold the proteins and provide a glimpse of the intermediate states. Here, we observe the high resolution structure of a hydrophobic core mutant of Ubiquitin at an extreme acidic pH by nuclear magnetic...
nmrlearner
Journal club
0
05-18-2016 08:30 AM
[NMR paper] Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.
Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.
Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.
Protein Sci. 2016 Apr 25;
Authors: Surana P, Das R
Abstract
The study of intermediates in the protein folding pathway provides a wealth of information about the energy landscape. The intermediates also frequently initiate pathogenic fibril formations. While observing the intermediates is difficult due to their transient nature, extreme conditions can partially unfold the...
nmrlearner
Journal club
0
04-26-2016 12:14 PM
Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR
Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR
Abstract
The study of intermediates in the protein folding pathway provides a wealth of information about the energy landscape. The intermediates also frequently initiate pathogenic fibril formations. While observing the intermediates is difficult due to their transient nature, extreme conditions can partially unfold the proteins and provide a glimpse of the intermediate states. Here, we observe the high resolution structure of a hydrophobic core mutant of Ubiquitin at an extreme acidic pH by Nuclear Magnetic...