Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations - Science Advances
Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations - Science Advances
Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations Science AdvancesWe present an integrated experimental and computational approach for de novo protein structure determination in which short-distance cross-linking data are ...
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nmrlearner
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03-24-2019 10:41 PM
SwissFEL makes protein structures visible - Phys.Org
SwissFEL makes protein structures visible - Phys.Org
SwissFEL makes protein structures visible Phys.OrgFor the development of new medicinal agents, accurate knowledge of biological processes in the body is a prerequisite. Here proteins play a crucial role.
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nmrlearner
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01-07-2019 05:49 AM
[Question from NMRWiki Q&A forum] What are the biggest differences in solving NMR structures of DNA or RNA vs. proteins?
What are the biggest differences in solving NMR structures of DNA or RNA vs. proteins?
I've only solved NMR structure of globular proteins (actually in a complex with a short stretch of DNA), but never a structure of nucleic acid alone.
What are (are there?) the major differences in the approaches when working on a structure of nucleic acid - in terms of choice of the NMR technique, maybe specific parameters and structure simulation?
Are distance restraints alone sufficient to obtain structure of DNA or RNA?
Thank you in advance!
nmrlearner
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06-28-2016 04:38 AM
[NMR images] Solving protein structures by NMR
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27/06/2013 2:11:12 PM GMT
Solving protein structures by NMR
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nmrlearner
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06-27-2013 02:10 PM
[Question from NMRWiki Q&A forum] How would you compare solving NMR structure of a smaller peptide vs that of globular protein?
How would you compare solving NMR structure of a smaller peptide vs that of globular protein?
By smaller peptide I mean somewhere around 15-20 aminoacids, having a cycle or two that constrain the geometry.
Also - I am interested in getting as much detail about the structure of the peptide as possible.
Do you typically need to record NOE buildup curves in such cases?
Given that side-chains of the peptide are unlikely to be packed like in the core of the globular protein - do you include side-chain NOE's into structure calculations?