[NMR paper] Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Related Articles Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
J Biomol NMR. 2013 Apr 23;
Authors: Chakravorty DK, Wang B, Lee CW, Guerra AJ, Giedroc DP, Merz KM
Abstract
Correctly calculating the structure of metal coordination sites in a protein during the process of nuclear magnetic resonance (NMR) structure determination and refinement continues to...
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[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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Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 215</br>
Claudio Luchinat, Malini Nagulapalli, Giacomo Parigi, Luca Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively placed...
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03-09-2012 09:16 AM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 30 December 2011</br>
Claudio*Luchinat, Malini*Nagulapalli, Giacomo*Parigi, Luca*Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively...
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12-31-2011 10:40 AM
[NMR paper] NMR identification of heavy metal-binding sites in a synthetic zinc finger peptide: t
NMR identification of heavy metal-binding sites in a synthetic zinc finger peptide: toxicological implications for the interactions of xenobiotic metals with zinc finger proteins.
Related Articles NMR identification of heavy metal-binding sites in a synthetic zinc finger peptide: toxicological implications for the interactions of xenobiotic metals with zinc finger proteins.
Toxicol Appl Pharmacol. 2001 Apr 1;172(1):1-10
Authors: Razmiafshari M, Kao J, d'Avignon A, Zawia NH
Lead (Pb), mercury (Hg), and cadmium (Cd) are toxic and interfere with...
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[NMR paper] Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein C
Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains.
Related Articles Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains.
J Mol Biol. 1999 Oct 1;292(4):893-908
Authors: Kloiber K, Weiskirchen R, Kräutler B, Bister K, Konrat R
The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been...
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[NMR paper] Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region o
Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
J Biol Chem. 1995 Apr 7;270(14):7980-7
Authors: Freedman SJ, Furie BC, Furie B, Baleja JD
The gamma-carboxyglutamic acid-rich...