Related ArticlesStructure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
Biochemistry. 1996 Jun 18;35(24):7684-91
Authors: Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE
As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization.
[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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[NMR paper] NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
Related Articles NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
Eur J Biochem. 1999 Dec;266(2):359-69
Authors: Wecker K, Roques BP
The human immunodeficiency virus type 1 (HIV-1) genome encodes a highly conserved 16 kDa regulatory gene product, Vpr (viral protein of regulation, 96 amino acid residues), which is incorporated into virions, in quantities equivalent to those of the viral Gag proteins. In the infected cells, Vpr is...
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[NMR paper] The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA bindi
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
Related Articles The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
J Mol Biol. 1999 Jul 9;290(2):495-504
Authors: Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T
Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA protein, and functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential for cell viability. The...
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[NMR paper] Determination of the structure of the N-terminal splice region of the cyclic AMP-spec
Determination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructs.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Determination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructs.
...
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[NMR paper] NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Ev
NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Related Articles NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Biochemistry. 1994 May 17;33(19):6004-14
Authors: Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL
The solution structure of the isolated N-terminal fragment of streptococcal protein-G B1 domain has been...
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[NMR paper] NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Ev
NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Related Articles NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation.
Biochemistry. 1994 May 17;33(19):6004-14
Authors: Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL
The solution structure of the isolated N-terminal fragment of streptococcal protein-G B1 domain has been...
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[NMR paper] Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2
Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR.
Related Articles Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR.
J Biochem. 1993 Sep;114(3):421-31
Authors: Lancelin JM, Stein M, Jacquot JP
The recombinant form of the chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii that preferentially activates the NADP...
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[NMR paper] NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: m
NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions.
J Mol Biol. 1999 Feb 5;285(5):2105-17
Authors: Schüler W, Wecker K, de Rocquigny H, Baudat Y, Sire J, Roques BP
The HIV-1 regulatory protein Vpr (96 amino...
Structure determination of the N-terminal thioredoxin-like domain of protein disulfid
Linear Mode
