Related ArticlesSequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
Biochemistry. 1991 Feb 12;30(6):1663-72
Authors: Constantine KL, Ramesh V, Bányai L, Trexler M, Patthy L, Llinás M
Sequence-specific resonance assignments for the isolated second or b domain of the bovine seminal fluid protein PDC-109 have been obtained from analysis of two-dimensional 1H NMR experiments recorded at 500 MHz. These assignments include the identification of all aromatic and most aliphatic amino acid resonances. Stereospecific assignment of resonances stemming from the Val2 CH3 gamma,gamma' groups and from seven CH beta,beta' geminal pairs has been accomplished by analysis of 3J alpha beta coupling constants in conjunction with patterns of cross-peak intensities observed in two-dimensional nuclear Overhauser effect (NOESY) spectra. Analysis of NOESY and 3J alpha NH data reveals a small antiparallel beta-sheet involving stretches containing residues 25-28 and 39-42, a cis-proline residue (Pro4), antiparallel strands consisting of residues 1-3, 5-7, and 10-13, and an aromatic cluster composed of Tyr7, Trp26, and Tyr33. The results of distance geometry and restrained molecular dynamics calculations indicate that the global fold of the PDC-109 b domain, a type II module related to those found in fibronectin, is somewhat different from that predicted by modeling the structure on the basis of homology between type II and kringle units. A shallow depression in the molecular surface which presents a solvent-exposed hydrophobic area--a potential ligand-binding site-is identified in the NMR-based models.
[NMR paper] Sequence-specific resonance assignments of the 1H-NMR spectra and structural characte
Sequence-specific resonance assignments of the 1H-NMR spectra and structural characterization in solution of the HIV-1 transframe protein p6.
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 Sequence-specific resonance assignments of the 1H-NMR spectra and structural characterization in solution of the HIV-1 transframe protein p6.
Eur J Biochem. 1996 Apr 15;237(2):383-92
Authors: Beissinger M, Paulus C, Bayer P, Wolf H, Rösch P, Wagner R
...
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[NMR paper] Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT
Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR.
Related Articles Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR.
Biochemistry. 1993 Dec 7;32(48):13071-80
Authors: Abeygunawardana C, Weber DJ, Frick DN, Bessman MJ, Mildvan AS
The MutT protein, a 129-residue enzyme from Escherichia coli which prevents A.T-->C.G mutations, catalyzes the hydrolysis of nucleoside triphosphates (NTP)...
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[NMR paper] Sequence-specific 1H-NMR assignments and folding topology of human CD59.
Sequence-specific 1H-NMR assignments and folding topology of human CD59.
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 Sequence-specific 1H-NMR assignments and folding topology of human CD59.
Protein Sci. 1993 Dec;2(12):2015-27
Authors: Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D
CD59 is a recently...
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[NMR paper] Sequence-specific 1H NMR assignments and secondary structure of the streptococcal pro
Sequence-specific 1H NMR assignments and secondary structure of the streptococcal protein G B2-domain.
Related Articles Sequence-specific 1H NMR assignments and secondary structure of the streptococcal protein G B2-domain.
Biochemistry. 1992 Apr 14;31(14):3604-11
Authors: Orban J, Alexander P, Bryan P
Two-dimensional NMR spectroscopy has been used to obtain sequence-specific 1H NMR assignments for the IgG-binding B2-domain of streptococcal protein G. Secondary structure elements were identified from analysis of characteristic backbone-backbone...
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[NMR paper] Sequence-specific NMR assignments of the trp repressor from Escherichia coli using th
Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
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 Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
Eur J Biochem. 1992 Feb 15;204(1):137-46
Authors: Borden KL, Bauer CJ, Frenkiel TA, Beckmann P, Lane AN
...
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[NMR paper] Sequence-specific 1H NMR assignments and determination of the secondary structure for
Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.
Related Articles Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.
Biochemistry. 1990 Aug 14;29(32):7515-22
Authors: Vendrell J, Wider G, Avilés FX, Wüthrich K
Nearly complete sequence-specific 1H NMR assignments are presented for amino acid residues 3-81 in the 81-residue globular...
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[NMR paper] Complete sequence-specific 1H NMR assignments for human insulin.
Complete sequence-specific 1H NMR assignments for human insulin.
Related Articles Complete sequence-specific 1H NMR assignments for human insulin.
Biochemistry. 1990 Mar 27;29(12):2906-13
Authors: Kline AD, Justice RM
Solvent conditions where human insulin could be studied by high-resolution NMR were determined. Both low pH and addition of acetonitrile were required to overcome the protein's self-association and to obtain useful spectra. Two hundred eighty-six 1H resonances were located and assigned to specific sites on the protein by using...
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[NMR paper] Sequence-specific 1H NMR assignments and secondary structure of eglin c.
Sequence-specific 1H NMR assignments and secondary structure of eglin c.
Related Articles Sequence-specific 1H NMR assignments and secondary structure of eglin c.
Biochemistry. 1990 Feb 13;29(6):1465-74
Authors: Hyberts SG, Wagner G
Sequence-specific nuclear magnetic resonance assignments were obtained for eglin c, a polypeptide inhibitor of the granulocytic proteinases elastase and cathepsin G and some other proteinases. The protein consists of a single polypeptide chain of 70 residues. All proton resonances were assigned except for some...