Related ArticlesChanges in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements.
J Am Chem Soc. 2005 Jan 26;127(3):828-9
Authors: Wang T, Frederick KK, Igumenova TI, Wand AJ, Zuiderweg ER
The fast dynamics of protein backbones are often investigated by nuclear magnetic relaxation experiments that report on the degree of spatial restriction of the amide bond vector. By comparing calmodulin in the peptide-bound and peptide-free states with these classical methods, we observe little difference in the dynamics of the polypeptide main chain (average order parameter decrease of 0.01 unit upon binding). However, when using NMR methods that monitor the mobility of the CO-Calpha bond vector, we reveal a significant reduction of dynamics of the protein main chain (average order parameter decrease of 0.048 units). Previous investigations have suggested that the side-chain dynamics is reduced by an average of 0.07 order parameter units upon ligand binding (Lee, A. L.; Kinnear, S. A.; Wand, A. J. Nat. Struct. Biol. 2000, 7, 72-77). The current findings suggest that the change of the CO-Calpha bond vector dynamics is intermediate between the changes in NH and side-chain dynamics and report a previously undetected loss of main-chain entropy. Weak site-to-site correlations between the different motional indicators are also observed.
[NMR paper] NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Related Articles NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Biochemistry. 2005 Sep 6;44(35):11766-76
Authors: Naik MT, Lee H, Bracken C, Breslow E
Neurophysins are hormone-binding proteins composed of two partially homologous domains. Ligand-binding (localized to the...
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[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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[NMR paper] A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-cor
A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
Related Articles A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
J Mol Biol. 1998 Mar 13;276(5):939-54
Authors: Yang D, Mittermaier A, Mok YK, Kay LE
Two new NMR experiments are presented for measuring side-chain dynamics in proteins. The first method, requiring 15N, 13C,...
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[NMR paper] Main-chain dynamics of cardiotoxin II from Taiwan cobra (Naja naja atra) as studied b
Main-chain dynamics of cardiotoxin II from Taiwan cobra (Naja naja atra) as studied by carbon-13 NMR at natural abundance: delineation of the role of functionally important residues.
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Biochemistry. 1998 Jan 6;37(1):155-64
Authors: Lee CS, Kumar TK, Lian LY, Cheng JW, Yu C
Cardiotoxin analogue II (CTX II) is an all beta-sheet, small molecular mass...
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[NMR paper] Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of
Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol.
J Mol Biol. 1996 Apr 5;257(3):669-83
Authors: Buck M, Schwalbe H, Dobson CM
15N NMR relaxation measurements have been used to study the dynamic...
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[NMR paper] NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-c
NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin.
Protein Sci. 1996 Dec;5(12):2552-65
Authors: De Lorimier...
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[NMR paper] Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by m
Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and 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 Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy.
J Biol Chem. 1995 Sep 1;270(35):20643-52
Authors: Moser MJ, Lee SY, Klevit RE, Davis TN
As a first step toward identifying the important structural elements of...