Protein side chain dynamics play a vital role in many biological processes, but differentiating mobile from rigid side chains remains a technical challenge in structural biology. Solution NMR spectroscopy is ideally suited for this but suffers from limited signal-to-noise, signal overlap, and a need for fractional ^(13)C or ²H labeling. Here we introduce a simple strategy measuring initial ¹H relaxation rates during a ¹H TOCSY sequence like DIPSI-2, which can be appended to the beginning of any...
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain
Abstract
Protein side chain dynamics play a vital role in many biological processes, but differentiating mobile from rigid side chains remains a technical challenge in structural biology. Solution NMR spectroscopy is ideally suited for this but suffers from limited signal-to-noise, signal overlap, and a need for fractional 13C or 2H labeling. Here we introduce a simple strategy measuring initial 1H relaxation rates during a 1H TOCSY sequence like DIPSI-2,...
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07-22-2022 11:46 PM
[NMR images] Side-chain assignment with a 15N-TOCSY-HSQC spectrum
http://www.protein-nmr.org.uk/pictures/assign_theory/assign_15ntocsy_principle.png
8/04/2014 7:46:05 AM GMT
Side-chain assignment with a 15N-TOCSY-HSQC spectrum
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04-08-2014 07:45 AM
[NMR paper] A simple method to measure protein side-chain mobility using NMR chemical shifts.
A simple method to measure protein side-chain mobility using NMR chemical shifts.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A simple method to measure protein side-chain mobility using NMR chemical shifts.
J Am Chem Soc. 2013 Sep 13;
Authors: Berjanskii MV, Wishart DS
Abstract
Protein side-chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein-protein,...
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09-17-2013 11:36 PM
[NMR paper] Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Biomol NMR Assign. 2013 Jan 22;
Authors: Orbán-Németh Z, Henen MA, Geist L, Zerko S, Saxena S, Stanek J, Ko?mi?ski W, Propst F, Konrat R
Abstract
Microtubule-associated protein 1B (MAP1B) is a classical...
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02-03-2013 10:19 AM
Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data
Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data
Abstract One bottleneck in NMR structure determination lies in the laborious and time-consuming process of side-chain resonance and NOE assignments. Compared to the well-studied backbone resonance assignment problem, automated side-chain resonance and NOE assignments are relatively less explored. Most NOE assignment algorithms require nearly complete side-chain resonance assignments from a series of through-bond experiments such as HCCH-TOCSY or HCCCONH. Unfortunately, these TOCSY...
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06-27-2011 04:30 AM
[NMR paper] Relating side-chain mobility in proteins to rotameric transitions: insights from mole
Relating side-chain mobility in proteins to rotameric transitions: insights from molecular dynamics simulations and NMR.
Related Articles Relating side-chain mobility in proteins to rotameric transitions: insights from molecular dynamics simulations and NMR.
J Biomol NMR. 2005 Jun;32(2):151-62
Authors: Hu H, Hermans J, Lee AL
The dynamic aspect of proteins is fundamental to understanding protein stability and function. One of the goals of NMR studies of side-chain dynamics in proteins is to relate spin relaxation rates to discrete...
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11-25-2010 08:21 PM
[NMR paper] Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on B
Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on Brownian dynamic simulations.
Related Articles Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on Brownian dynamic simulations.
J Biomol NMR. 2004 May;29(1):21-35
Authors: Bernadó P, Fernandes MX, Jacobs DM, Fiebig K, García de la Torre J, Pons M
Many important proteins contain multiple domains connected by flexible linkers. Inter-domain motion is suggested to play a key role in many processes involving molecular recognition....
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11-24-2010 09:51 PM
[NMR paper] Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studi
Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Related Articles Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Biochemistry. 2001 Jun 5;40(22):6559-69
Authors: Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is...
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain
Linear Mode
