Related ArticlesSequential 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: structural changes between the free B domain in solution and the Fc-bound B domain in crystal.
Biochemistry. 1990 Sep 18;29(37):8787-93
Authors: Torigoe H, Shimada I, Saito A, Sato M, Arata Y
The recombinant B domain (FB) of staphylococcal protein A, which specifically binds to the Fc portion of immunoglobulin G (IgG), has been investigated with the use of two-dimensional proton nuclear magnetic resonance spectroscopy. All backbone and side-chain proton resonances of FB (60 amino acid residues), except the amide proton resonance of Ala2, were assigned by the sequential assignment procedures by using double-quantum-filtered correlated spectroscopy (DQF-COSY), homonuclear Hartmann-Hahn spectroscopy (HOHAHA), and nuclear Overhauser enhancement spectroscopy (NOESY). On the basis of the NOESY data, three helical regions, Glu9-His19, Glu25-Asp37, and Ser42-Ala55, were identified in the free FB in solution. Existence of two of the three helical regions, Glu9-His19 and Glu25-Asp37, in consistent with the X-ray crystallographic structure of the Fc-bound FB [Deisenhofer, J. (1981) Biochemistry 20, 2361-2370]. By contrast, in the Fc-bound FB as revealed by the X-ray analysis, the Ser42-Glu48 segment is extended and no structural information has been available in the Ala49-Ala55 segment. We suggest that a significant conformation change is induced in the C-terminal region of FB when it is bound to the Fc portion of IgG.
[NMR paper] Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronu
Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronuclear NMR spectroscopy.
Related Articles Chemical shift assignments and secondary structure of the Grb2 SH2 domain by heteronuclear NMR spectroscopy.
J Biomol NMR. 1996 Mar;7(2):89-98
Authors: Wang YS, Frederick AF, Senior MM, Lyons BA, Black S, Kirschmeier P, Perkins LM, Wilson O
The growth factor receptor-bound protein-2 (Grb-2) is an adaptor protein that mediates signal transduction pathways. Chemical shift assignments were obtained for the SH2 domain of...
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[NMR paper] Sequential assignments and identification of secondary structure elements of the coli
Sequential assignments and identification of secondary structure elements of the colicin E9 immunity protein in solution by homonuclear and heteronuclear NMR.
Related Articles Sequential assignments and identification of secondary structure elements of the colicin E9 immunity protein in solution by homonuclear and heteronuclear NMR.
Biochemistry. 1994 Oct 18;33(41):12347-55
Authors: Osborne MJ, Lian LY, Wallis R, Reilly A, James R, Kleanthous C, Moore GR
1H-1H, 1H-15N, and 1H-1H-15N multidimensional NMR spectroscopic studies of the 86 amino...
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[NMR paper] Sequential 1H and 15N NMR assignments and secondary structure of a recombinant anti-d
Sequential 1H and 15N NMR assignments and secondary structure of a recombinant anti-digoxin antibody VL domain.
Related Articles Sequential 1H and 15N NMR assignments and secondary structure of a recombinant anti-digoxin antibody VL domain.
Biochemistry. 1992 Jun 2;31(21):5033-43
Authors: Constantine KL, Goldfarb V, Wittekind M, Anthony J, Ng SC, Mueller L
A uniformly 15N-labeled recombinant light-chain variable (VL) domain from the anti-digoxin antibody 26-10 has been investigated by heteronuclear two-dimensional (2D) and three-dimensional...
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[NMR paper] 1H NMR sequential assignments and identification of secondary structural elements in
1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas.
Related Articles 1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas.
Biochemistry. 1992 Feb 25;31(7):1961-8
Authors: Ye XM, Pochapsky TC, Pochapsky SS
Sequential 1H resonance assignments and secondary structural features of putidaredoxin (Pdx), a 106-residue globular protein consisting of...
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[NMR paper] Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from p
Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Related Articles Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Biochemistry. 1991 Jun 4;30(22):5335-40
Authors: Lian LY, Yang JC, Derrick JP, Sutcliffe MJ, Roberts GC, Murphy JP, Goward CR, Atkinson T
Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6988, which retains IgG-binding activity, has been...
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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] NMR assignments and secondary structure of the UvrC binding domain of UvrB.
NMR assignments and secondary structure of the UvrC binding domain of UvrB.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR assignments and secondary structure of the UvrC binding domain of UvrB.
FEBS Lett. 1999 May 21;451(2):181-5
Authors: Alexandrovich A, Sanderson MR, Moolenaar GF, Goosen N, Lane AN
The 55 residue C-terminal domain of UvrB that interacts with UvrC during excision repair in Escherichia coli has been expressed and purified as a (His)6 fusion...
Sequential 1H NMR assignments and secondary structure of the B domain of staphylococc
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