Related ArticlesSolution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor PKI(6-22), the substrate [Ala20-Ser21]PKI(5-24), and a phosphorylated form of the latter [Ala20-Ser21P]PKI(5-24). A homologous fold was found in the three peptides which consisted of an N-terminal segment in helical conformation to residue 13 and a C-terminal segment poorly defined conformationally. A parallel study was carried out by molecular dynamics (MD) for the inhibitor peptide PKI(5-24). The N-terminal helix, as observed in the crystal structure of the catalytic subunit-PKI(5-24) complex, was conserved in the MD simulations with the enzyme-free inhibitor. Similarly the Gly14-Gly17 turn was apparent in all MD structures, whereas the C-terminal region, residues 18-24, was directed towards the N-terminal helix in contrast to the extended conformation of this segment pointing away from the N-terminal helix in the crystal structure. This is primarily due to ionic interaction between Asp9 and Arg15. Indeed, a detailed analysis of the NOE contacts by NOESY at low temperature (2 degrees C) shows the occurrence of pH-dependent contacts with Phe10. We conclude that the binding of short inhibitors, such as PKI(5-24), to the enzyme involves a conformational rearrangement of the C-terminal region. The substrate [Ala20-Ser21]PKI(5-24) and the product [Ala20-Ser21P]PKI(5-24), give very similar structures with local rearrangements involving some of the side chains.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Related Articles Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Peptides. 2002 Dec;23(12):2127-41
Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S
The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the...
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[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro
Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...
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08-22-2010 03:31 PM
[NMR paper] The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of
The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of the folding of a synthetic model for the DNA-binding loop of the ssDNA-binding protein encoded by gene V of phage 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 The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of the folding of a synthetic model for the DNA-binding loop of the ssDNA-binding protein encoded by gene V of phage M13.
Eur...
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[NMR paper] NMR solution structure of a synthetic troponin C heterodimeric domain.
NMR solution structure of a synthetic troponin C heterodimeric domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR solution structure of a synthetic troponin C heterodimeric domain.
Biochemistry. 1996 Jun 11;35(23):7429-38
Authors: Shaw GS, Sykes BD
The C-terminal domain from the muscle protein troponin C (TnC) comprises two helix-loop-helix calcium-binding sites (residues 90-162). The assembly of these two sites is governed by calcium binding enabling a synthetic C-terminal...
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[NMR paper] Solution structure determination by NMR spectroscopy of a synthetic peptide correspon
Solution structure determination by NMR spectroscopy of a synthetic peptide corresponding to a putative amphipathic alpha-helix of spiralin: resonance assignment, distance geometry and simulated annealing.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structure determination by NMR spectroscopy of a synthetic peptide corresponding to a putative amphipathic alpha-helix of spiralin: resonance assignment, distance geometry and simulated annealing.
Biochim Biophys Acta. 1995 May...
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[NMR paper] NMR-derived solution conformations of a hybrid synthetic peptide containing multiple
NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
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Biochemistry. 1994 Mar 1;33(8):2055-62
Authors: de Lorimier R, Moody MA, Haynes BF, Spicer LD
Solution conformations of a 40-residue hybrid peptide containing T-helper epitopes and B-cell...
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[NMR paper] NMR-derived solution conformations of a hybrid synthetic peptide containing multiple
NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Related Articles NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Biochemistry. 1994 Mar 1;33(8):2055-62
Authors: de Lorimier R, Moody MA, Haynes BF, Spicer LD
Solution conformations of a 40-residue hybrid peptide containing T-helper epitopes and B-cell...