Related ArticlesSequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy.
Protein Sci. 1998 Nov;7(11):2421-30
Authors: Qian H, Rogers MS, Schleucher J, Edlund U, Strehler EE, Sethson I
Human calmodulin-like protein (CLP) is closely related to vertebrate calmodulin, yet its unique cell specific expression pattern, overlapping but divergent biochemical properties, and specific target proteins suggest that it is not an isoform of calmodulin. To gain insight into the structural differences that may underlie the difference target specificities and biochemical properties of CLP when compared to calmodulin, we determined the sequential backbone assignment and associated secondary structure of 144 out of the 148 residues of Ca2+-CLP by using multinuclear multidimensional NMR spectroscopy. Despite a very high overall degree of structural similarity between CLP and calmodulin, a number of significant differences were found mainly in the length of alpha-helices and in the central nonhelical flexible region. Interestingly, the regions of greatest primary sequence divergence between CLP and calmodulin in helices III and VIII displayed only minor secondary structure differences. The data suggest that the distinct differences in target specificity and biochemical properties of CLP and calmodulin result from the sum of several minor structural and side-chain changes spread over multiple domains in these proteins.
[NMR paper] Sequential 1H and 15N NMR resonance assignment and secondary structure of ferrocytoch
Sequential 1H and 15N NMR resonance assignment and secondary structure of ferrocytochrome c2 from Rhodobacter sphaeroides.
Related Articles Sequential 1H and 15N NMR resonance assignment and secondary structure of ferrocytochrome c2 from Rhodobacter sphaeroides.
J Biochem. 1996 Jun;119(6):1131-42
Authors: Gans P, Simorre JP, Caffrey M, Marion D, Richaud P, Verméglio A
Sequence-specific 1H and 15N assignments have been made for the amino acids of the ferrocytochrome c2 from Rhodobacter sphaeroides. Initial assignments were made by analysis of...
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[NMR paper] Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by
Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
Related Articles Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
J Biomol NMR. 1996 Dec;8(4):417-28
Authors: Sethson I, Edlund U, Holak TA, Ross A, Jonsson BH
The backbone NMR resonances of human carbonic anhydrase I (HCA I) have been assigned. This protein is one of...
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[NMR paper] Use of graph theory for secondary structure recognition and sequential assignment in
Use of graph theory for secondary structure recognition and sequential assignment in heteronuclear (13C, 15N) NMR spectra: application to HU protein from Bacillus stearothermophilus.
Related Articles Use of graph theory for secondary structure recognition and sequential assignment in heteronuclear (13C, 15N) NMR spectra: application to HU protein from Bacillus stearothermophilus.
Biopolymers. 1996 Nov;39(5):691-707
Authors: van Geerestein-Ujah EC, Mariani M, Vis H, Boelens R, Kaptein R
A computer-assisted procedure, based upon a branch of...
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[NMR paper] Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a dou
Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen.
FEBS Lett. 1995 Apr 10;362(3):333-6
Authors: Bycroft M, Proctor M, Freund SM, St Johnston D
NMR spectroscopy has been...
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[NMR paper] Assignment of the backbone 1H and 15N NMR resonances and secondary structure characte
Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar.
FEBS Lett. 1993 Oct 11;332(1-2):81-7
Authors: Lubienski MJ, Bycroft M, Jones DN, Fersht AR
Barstar, a polypeptide inhibitor of ribonucleases, has been studied by 2D and 3D NMR techniques using uniformly...
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[NMR paper] 1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-
1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution.
Related Articles 1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution.
J Biochem. 1992 Apr;111(4):529-36
Authors: Sato A, Nishimura S, Ohkubo T, Kyogoku Y, Koyama S, Kobayashi M, Yasuda T, Kobayashi Y
Human insulin-like growth factor-I (IGF-I) was studied by two-dimensional 1H-NMR spectroscopy. Resonance assignments were obtained for all the backbone protons and almost all of the sidechain protons...
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[NMR paper] Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonu
Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1991 Jun 18;30(24):6036-47
Authors: Yamazaki T, Yoshida M, Kanaya S, Nakamura H, Nagayama K
The assignments of individual magnetic resonances of backbone nuclei of a larger...
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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...