Related ArticlesNMR 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 R, Hellinga HW, Spicer LD
Core-packing mutants of proteins often approach molten globule states, and hence may have attributes of folding intermediates. We have studied a core-packing mutant of thioredoxin, L78K, in which a leucine residue is substituted by lysine, using 15N heteronuclear two- and three-dimensional NMR. Chemical shift differences between the mutant and wild-type main-chain resonances reveal that structural changes caused by the mutation are localized within 12 A of the altered side chain. The majority of resonances are unchanged, as are many 1H-1H NOEs indicative of the main-chain fold, suggesting that the structure of L78K is largely similar to wild type. Hydrogen exchange studies reveal that residues comprising the central beta-sheet of both mutant and wild-type proteins constitute a local unfolding unit, but with the unfolding/folding equilibrium approximately 12 times larger in L78K. The dynamics of main-chain NH bonds in L78K were studied by 15N spin relaxation and compared with a previous study of wild type. Order parameters for angular motion of NH bonds in the mutant are on average lower than in wild type, suggesting greater spatial freedom on a rapid time scale, but may also be related to different rotational correlation times in the two proteins. There is also evidence of greater conformational exchange in the mutant. Differences between mutant and wild type in hydrogen exchange and main-chain dynamics are not confined to the vicinity of the mutation. We infer that mispacking of the protein core in one location affects local dynamics and stability throughout.
[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] Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-corre
Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements.
Related Articles Changes 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...
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[NMR paper] NMR-detected hydrogen exchange and molecular dynamics simulations provide structural
NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126.
Related Articles NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126.
Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14790-5
Authors: Kuwata K, Matumoto T, Cheng H, Nagayama K, James TL, Roder H
PrP106-126, a peptide corresponding to residues 107-127 of the human prion protein, induces neuronal cell...
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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] 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...
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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] Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA meth
Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA methylphosphotriester repair domain of Escherichia coli Ada using NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA methylphosphotriester repair domain of Escherichia coli Ada using NMR.
Biochemistry. 1996 Jul 23;35(29):9335-48
Authors: Habazettl J, Myers LC, Yuan F, Verdine GL, Wagner G
The 10kDa amino-terminal fragment of...