Related ArticlesSolution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Biomol NMR Assign. 2014 Jan 12;
Authors: Rostkova E, Gautel M, Pfuhl M
Abstract
The regulatory light chain (RLC) of striated and cardiac muscle myosin plays a complex role in muscle function and regulation. Together with the essential light chain it provides stability to the lever arm, which is essential for force generation. Furthermore, phosphorylation and interaction with myosin binding protein C (MyBP-C) suggest an additional role in the regulation of muscle contraction. The former is of particular importance in the heart, where RLC phosphorylation appears to be correlated to the wringing motion of heart contraction. To address these questions and because of a lack of mammalian RLC structures, we initiated an NMR study of the human cardiac regulatory myosin light chain.
PMID: 24414277 [PubMed - as supplied by publisher]
[NMR paper] (15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
(15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles (15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
Biomol NMR Assign. 2013 Jan 29;
Authors: Prosser CE, Waters LC, Muskett FW, Veverka V, Addis PW, Griffin LM, Baker TS,...
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[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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‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy
‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 25 October 2011</br>
Woo Sung*Son, Sang Ho*Park, Henry J.*Nothnagel, George J.*Lu, Yan*Wang, ...</br>
‘q-titration’ refers to the systematic comparison of signal intensities in solution NMR spectra of uniformlyN labeled membrane proteins solubilized in micelles and isotropic bicelles as a function of the molar ratios (q) of the...
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10-26-2011 11:25 AM
[Question from NMRWiki Q&A forum] Side chain assignment of C-terminal residue
Side chain assignment of C-terminal residue
Dear Friends,
I am not able to figure out how to determine the side chain assignment of Last C-terminal SERINE residue of my protein. I can determine CA, CB, CO, N,H values from HNCA, CBCANH, HNCACO. Can someone tell which experiment will give me the information of HA, HB2 and HB3
Regards
Arun
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10-09-2011 06:23 PM
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
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5.
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5.
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5.
J Mol Biol. 2010 Dec 14;
Authors: Chagot B, Chazin WJ
The function of the human voltage-gated sodium channel Na(V)1.5 is regulated in part by intracellular calcium signals. The ubiquitous calcium sensor protein calmodulin (CaM) is an important part of the complex calcium-sensing apparatus in Na(V)1.5. CaM interacts with an IQ...
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12-21-2010 01:00 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...
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11-19-2010 08:32 PM
[NMR paper] Detection of very weak side chain-main chain hydrogen bonding interactions in medium-
Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy.
Related Articles Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy.
J Biomol NMR. 2000 May;17(1):79-82
Authors: Liu A, Hu W, Majumdar A, Rosen MK, Patel DJ
We describe the direct observation of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled...