Related ArticlesNMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation.
Proteins. 1995 May;22(1):41-4
Authors: Tasayco ML, Chao K
The study of complementary protein fragments is thought to be generally useful to identify early folding intermediates. A prerequisite for these studies is the reconstitution of the native-like structure by fragment complementation. Structural analysis of the complementation of the domain-sized proteolytic fragments of E. coli thioredoxin, using a combination of H-exchange and 2D NMR experiments as a fingerprint technique, provide evidence for the extensive reconstitution of a native beta-sheet, with local conformational adjustments near the cleavage site. Remarkably, the antiparallel beta-strand between the fragments shows a native-like protection of the amide protons to solvent exchange. Our results indicate that these fragments can be useful to study the early events in the still little understood formation of beta-sheets.
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Abstract We performed density functional calculations of backbone 15N shielding tensors in the regions of beta-sheet and turns of protein G. The calculations were carried out for all twenty-four beta-sheet residues and eight beta-turn residues in the protein GB3 and the results were compared with the available experimental data from solid-state and solution NMR measurements. Together with the alpha-helix data, our calculations cover 39 out of the 55 residues (or 71%) in GB3....
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[NMR paper] The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty
The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.
Related Articles The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.
Protein Sci. 2004 May;13(5):1227-37
Authors: Ogbay B, Dekoster GT, Cistola DP
Intestinal fatty acid-binding protein (I-FABP) has a clam-shaped structure that may serve as a scaffold for the design of artificial enzymes and drug carriers. In an attempt to optimize the scaffold for increased access to the...
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[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
J Mol Biol. 2003 May 16;328(5):1161-71
Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ
At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...
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[NMR paper] Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational
Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides.
Related Articles Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides.
J Pept Res. 2003 Apr;61(4):177-88
Authors: Santiveri CM, Rico M, Jiménez MA, Pastor MT, Pérez-Payá E
In a previous study we designed a 20-residue peptide able to adopt a significant population of a three-stranded...
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[NMR paper] Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics
Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
Related Articles Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
J Am Chem Soc. 2001 Jan 10;123(1):185-6
Authors: Stone MJ, Gupta S, Snyder N, Regan L
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[NMR paper] Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125
Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Related Articles Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Fold Des. 1998;3(5):313-20
Authors: Sharman GJ, Kenward N, Williams HE, Landon M, Mayer RJ, Searle MS
BACKGROUND: Transmissible spongiform encephalopathies are a group of neurodegenerative disorders of man and animals...
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[NMR paper] 2D 1H and 3D 1H-15N NMR of zinc-rubredoxins: contributions of the beta-sheet to therm
2D 1H and 3D 1H-15N NMR of zinc-rubredoxins: contributions of the beta-sheet to thermostability.
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 2D 1H and 3D 1H-15N NMR of zinc-rubredoxins: contributions of the beta-sheet to thermostability.
Protein Sci. 1996 May;5(5):883-94
Authors: Richie KA, Teng Q, Elkin CJ, Kurtz DM
...
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[NMR paper] 1H NMR identification of a beta-sheet structure and description of folding topology i
1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Related Articles 1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Biochemistry. 1991 Apr 23;30(16):3850-6
Authors: Pochapsky TC, Ye XM
Putidaredoxin (Pdx), a 106-residue globular protein consisting of a single polypeptide chain and a cluster, is the physiological reductant of P-450cam, which in turn catalyzes the monohydroxylation of camphor by molecular oxygen. No crystal structure has...
NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment compleme
Linear Mode
