Related ArticlesSequence-specific 1H NMR assignments, secondary structure, and location of the calcium binding site in the first epidermal growth factor like domain of blood coagulation factor IX.
Biochemistry. 1991 Jul 30;30(30):7402-9
Authors: Huang LH, Cheng H, Pardi A, Tam JP, Sweeney WV
Factor IX is a blood clotting protein that contains three regions, including a gamma-carboxyglutamic acid (Gla) domain, two tandemly connected epidermal growth factor like (EGF-like) domains, and a serine protease region. The protein exhibits a high-affinity calcium binding site in the first EGF-like domain, in addition to calcium binding in the Gla domain. The first EGF-like domain, factor IX (45-87), has been synthesized. Sequence-specific resonance assignment of the peptide has been made by using 2D NMR techniques, and its secondary structure has been determined. The protein is found to have two antiparallel beta-sheets, and preliminary distance geometry calculations indicate that the protein has two domains, separated by Trp28, with the overall structure being similar to that of EGF. An NMR investigation of the calcium-bound first EGF-like domain indicates the presence and location of a calcium binding site involving residues on both strands of one of the beta-sheets as well as the N-terminal region of the peptide. These results suggest that calcium binding in the first EGF-like domain could induce long-range (possibly interdomain) conformational changes in factor IX, rather than causing structural alterations in the EGF-like domain itself.
[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 1H-NMR assignments and secondary structure of the lipoyl domain of
Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
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 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
Eur J Biochem. 1991 Oct 1;201(1):203-9
Authors: Dardel F, Laue ED, Perham RN...
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[NMR paper] Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of
Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
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 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
Eur J Biochem. 1991 Oct 1;201(1):203-9
Authors: Dardel F, Laue ED, Perham RN...
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[NMR paper] Sequence-specific 1H NMR assignments, secondary structure, and location of the calciu
Sequence-specific 1H NMR assignments, secondary structure, and location of the calcium binding site in the first epidermal growth factor like domain of blood coagulation factor IX.
Related Articles Sequence-specific 1H NMR assignments, secondary structure, and location of the calcium binding site in the first epidermal growth factor like domain of blood coagulation factor IX.
Biochemistry. 1991 Jul 30;30(30):7402-9
Authors: Huang LH, Cheng H, Pardi A, Tam JP, Sweeney WV
Factor IX is a blood clotting protein that contains three regions,...
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08-21-2010 11:12 PM
[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] Sequence-specific 1H NMR assignments and secondary structure in solution of Escherich
Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.
Related Articles Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.
Biochemistry. 1990 Jul 10;29(27):6332-41
Authors: Arrowsmith CH, Pachter R, Altman RB, Iyer SB, Jardetzky O
Sequence-specific 1H NMR assignments are reported for the active L-tryptophan-bound form of Escherichia coli trp repressor. The repressor is a symmetric dimer of 107 residues per monomer; thus at 25 kDa, this...
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[NMR paper] Sequence-specific [1H]NMR resonance assignments and secondary structure identificatio
Sequence-specific NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
Related Articles Sequence-specific NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
FEBS Lett. 1990 Mar 26;262(2):179-84
Authors: Neuhaus D, Nakaseko Y, Nagai K, Klug A
Complete NMR resonance assignments are presented for the second of the three...
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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...