The homodimeric S100 protein calcyclin has been studied in the apo state by two-dimensional 1H NMR spectroscopy. Using a combination of scalar correlation and NOE experiments, sequence-specific 1H NMR assignments were obtained for all but one backbone and > 90% of the side-chain resonances. To our knowledge, the 2 x 90 residue (20 kDa) calcyclin dimer is the largest protein system for which such complete assignments have been made by purely homonuclear methods. Sequential and medium-range NOEs and slowly exchanging backbone amide protons identified directly the four helices and the short antiparallel beta-type interaction between the two binding loops that comprise each subunit of the dimer. Further analysis of NOEs enabled the unambiguous assignment of 556 intrasubunit distance constraints, 24 intrasubunit hydrogen bonding constraints, and 2 x 26 intersubunit distance constraints. The conformation of the monomer subunit was refined by distance geometry and restrained molecular dynamics calculations using the intrasubunit constraints only. Calculation of the dimer structure starting from this conformational ensemble has been reported elsewhere. The extent of structural homology among the apo calcyclin subunit, the monomer subunit of apo S100 beta, and monomeric apo calbindin D9k has been examined in detail by comparing 1H NMR chemical shifts and secondary structures. This analysis was extended to a comprehensive comparison of the three-dimensional structures of the calcyclin monomer subunit and calbindin D9k, which revealed greater similarity in the packing of their hydrophobic cores than was anticipated previously. Together, these results support the hypothesis that all members of the S100 family have similar core structures and similar modes of dimerization. Analysis of the amphiphilicity of Helix IV is used to explain why calbindin D9k is monomeric, but full-length S100 proteins form homodimers.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Prion. 2011 Jul 1;5(3)
Authors: Santo KP, Berjanskii M, Wishart DS, Stepanova M
Abstract
Collective motions on ns-?s time scales are known to have a major impact on protein folding, stability, binding and enzymatic efficiency. It is also believed that these motions may have an...
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Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Biochim Biophys Acta. 2011 Jul 23;
Authors: Cohen LS, Arshava B, Neumoin A, Becker JM, Güntert P, Zerbe O, Naider F
Fragments of integral membrane proteins have been used to study the physical chemical properties of regions of transporters and receptors. Ste2p(G31-T110) is an 80-residue polypeptide which contains a...
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Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative ¹³C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative ¹³C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative ¹³C NMR analysis of the products in wild-type and mutants.
J Biotechnol. 2011 Jan 10;151(1):30-42
Authors: Choi MH, Xu J, Gutierrez M, Yoo T, Cho YH, Yoon SC
Polyhydroxyalkanoic acids (PHAs) and rhamnolipids considered as biotechnologically important...
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[NMR paper] Automated analysis of protein NMR assignments and structures.
Automated analysis of protein NMR assignments and structures.
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Chem Rev. 2004 Aug;104(8):3541-56
Authors: Baran MC, Huang YJ, Moseley HN, Montelione GT
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[NMR paper] Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-label
Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning.
Related Articles Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning.
J Biomol NMR. 2004 Apr;28(4):311-25
Authors: Fujiwara T, Todokoro Y, Yanagishita H, Tawarayama M, Kohno T, Wakamatsu K, Akutsu H
Carbon-13 and nitrogen-15 signals of fully...
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[NMR paper] Automated analysis of NMR assignments and structures for proteins.
Automated analysis of NMR assignments and structures for proteins.
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Curr Opin Struct Biol. 1999 Oct;9(5):635-42
Authors: Moseley HN, Montelione GT
Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and...
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[NMR paper] 1H and 13C NMR assignments and structural aspects of a ferrocytochrome c-551 from the
1H and 13C NMR assignments and structural aspects of a ferrocytochrome c-551 from the purple phototrophic bacterium Ectothiorhodospira halophila.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H and 13C NMR assignments and structural aspects of a ferrocytochrome c-551 from the purple phototrophic bacterium Ectothiorhodospira halophila.
Eur J Biochem. 1995 Jan 15;227(1-2):249-60
Authors: Bersch B, Brutscher B, Meyer TE, Marion D
...
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[NMR paper] Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the
Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Related Articles Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Biochemistry. 1990 Sep 18;29(37):8797-804
Authors: Satterlee JD, Erman JE, Mauro JM, Kraut J
Proton NMR spectra of cytochrome c peroxidase (CcP) isolated from yeast (wild type) and two Escherichia coli...
1H NMR assignments of apo calcyclin and comparative structural analysis with calbindi
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