Related ArticlesSequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Biochem Cell Biol. 1998;76(2-3):267-75
Authors: Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we present the nuclear magnetic resonance spectra of native apoC-I and synthetic apoC-I, containing selected 15N-labelled amino acids, in the presence of sodium dodecyl sulfate. The proton resonances of apoC-I are assigned and the secondary structure is estimated from the difference of measured alpha-proton chemical shifts to random coil values and the observed NOE interactions. According to these data apoC-I forms two helices, Val-4-Lys-30 and Leu-34-Lys-52, linked by an unstructured region Gln-31-Glu-33. The N-terminal segments of each helix, Val-4-Gly-15 and Leu-34-Met-38, appear to be more flexible than the helical core regions Asn-16-Lys-30 and Arg-39-Lys-52.
[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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[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...