Related ArticlesSequence-specific 1H-NMR assignment and secondary structure of the Tyr41----His mutant of the single-stranded DNA binding protein, gene V protein, encoded by the filamentous bacteriophage M13.
Sequence-specific 1H-NMR assignments are reported for the Tyr41----His (Y41H) mutant of the single-stranded DNA binding protein, encoded by gene V of the filamentous bacteriophage M13 (GVP). The mutant protein was chosen for this purpose because it exhibits significantly improved solubility characteristics over wild-type GVP [Folkers et al. (1991) Eur. J. Biochem. 200, 139-148]. The secondary structure elements present in the protein are deduced from a qualitative interpretation of the nuclear Overhauser enhancement spectra and amide exchange data. The protein is entirely composed of antiparallel beta-structure. It is shown that identical structural elements are present in wild-type GVP. Previously, we have demonstrated that the secondary structure of the beta-loop, encompassing residues 13-31 which is present in GVP in solution, deviates from that proposed for the same amino acid sequence on the basis of X-ray diffraction data [van Duynhoven et al. (1990) FEBS Lett. 261, 1-4]. Now that we have arrived at a complete description of the secondary structure of the protein in solution, other deviations with respect to the crystallographically determined structure became apparent as well. The N-terminal part of the protein is, in solution, part of a triple-stranded beta-sheet while, in the crystal, it is an extended strand pointing away from the bulk of the protein dimer. One of the antiparallel beta-sheets in the protein which had been designated earlier as the complex loop has, in the solution structure, a different pairwise arrangement of the residues in its respective beta-ladders. Residues 30 and 48 are opposite to one another in the solution structure while in the crystal structure residues 32 and 48 are paired. A similar observation is made for the so-called dyad domain of the protein of which the beta-sheet in the solution structure is shifted by one residue with respect to that of the crystal structure.
[NMR paper] Sequence-specific 1H-NMR assignment and determination of the secondary structure of b
Sequence-specific 1H-NMR assignment and determination of the secondary structure of bovine heart fatty-acid-binding protein.
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 assignment and determination of the secondary structure of bovine heart fatty-acid-binding protein.
Eur J Biochem. 1992 Dec 15;210(3):901-10
Authors: Lücke C, Lassen D, Kreienkamp HJ, Spener F, Rüterjans H
The nearly complete...
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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 1H-NMR assignment and secondary structure of the Tyr41----His mutan
Sequence-specific 1H-NMR assignment and secondary structure of the Tyr41----His mutant of the single-stranded DNA binding protein, gene V protein, encoded by the filamentous bacteriophage M13.
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 assignment and secondary structure of the Tyr41----His mutant of the single-stranded DNA binding protein, gene V protein, encoded by the filamentous bacteriophage M13.
Eur J Biochem. 1991 Dec...
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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 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...