Recent advances in molecular modeling using deep learning can revolutionize our understanding of dynamic protein structures. NMR is particularly well-suited for determining dynamic features of biomolecular structures. The conventional process for determining biomolecular structures from experimental NMR data involves its representation as conformation-dependent restraints, followed by generation of structural models guided by these spatial restraints. Here we describe an alternative approach:...
[NMR paper] Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold
Structural Insights into the Dimeric Form of Bacillus subtilis RNase Y Using NMR and AlphaFold
RNase Y is a crucial component of genetic translation, acting as the key enzyme initiating mRNA decay in many Gram-positive bacteria. The N-terminal domain of Bacillus subtilis RNase Y (Nter-BsRNaseY) is thought to interact with various protein partners within a degradosome complex. Bioinformatics and biophysical analysis have previously shown that Nter-BsRNaseY, which is in equilibrium between a monomeric and a dimeric form, displays an elongated fold with a high content of ?-helices. Using...
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12-23-2022 07:50 PM
Hidden Structural Codes in Protein Intrinsic Disorder
Hidden Structural Codes in Protein Intrinsic Disorder
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00721/20171006/images/medium/bi-2017-00721n_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00721
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/mMCQe_lwg8U
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[NMR paper] Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.
Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.
Related Articles Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.
J Biomol Struct Dyn. 2015 Jan 14;:1-18
Authors: Naiyer A, Hassan MI, Islam A, Sundd M, Ahmad F
Abstract
Almost all proteins fold via a number of partially structured intermediates such as molten globule (MG) and pre-molten globule states. Understanding the structure of these intermediates at...
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Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion [Biophysics and Computational Biology]
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion
Meinhold, D. W., Wright, P. E....
Date: 2011-05-31
Detailed understanding of protein function and malfunction hinges on the ability to characterize transiently populated states and the transitions between them. Here, we use 15N, , and 13CO NMR R2 relaxation dispersion to investigate spontaneous unfolding and refolding events of native apomyoglobin. Above pH 5.0, dispersion is dominated by processes involving fluctuations of the F-helix region, which...
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Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
Proc Natl Acad Sci U S A. 2011 May 11;
Authors: Meinhold DW, Wright PE
Detailed understanding of protein function and malfunction hinges on the ability to characterize transiently populated states and the transitions between them. Here, we use (15)N, , and (13)CO NMR R(2)...
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05-13-2011 02:40 PM
[NMR paper] Structural analysis of non-native states of proteins by NMR methods.
Structural analysis of non-native states of proteins by NMR methods.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural analysis of non-native states of proteins by NMR methods.
Curr Opin Struct Biol. 1996 Feb;6(1):24-30
Authors: Shortle DR
Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, 15N and 13C resonances is often straightforward. Sensitive methods exist...
Hidden Structural States of Proteins Revealed by Conformer Selection with AlphaFold-NMR
Linear Mode
