Related ArticlesProbing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.
Biochemistry. 1991 Aug 27;30(34):8339-47
Authors: Shaw GS, Hodges RS, Sykes BD
Three 34-residue peptides corresponding to the high-affinity calcium-binding site III and two variant sequences from the muscle protein troponin C (TnC) were synthesized by solid-phase techniques. The two variant 34-residue peptides had amino acid modifications at either the coordinating positions or both the coordinating and noncoordinating positions, which corresponded to the residues found in the low-affinity calcium-binding site II of TnC. High-field 1H NMR spectroscopy was used to monitor calcium binding to each peptide to determine the effect these amino acid substitutions had on calcium affinity. The dissociation constant of the native site III peptide (SCIII) was 3 x 10(-6) M, smaller than that of the peptide incorporating the ligands from site II (LIIL), 8 x 10(-6) M, and that with the entire site II loop (LII), 3 x 10(-3) M, which bound calcium very weakly. These calcium dissociation constants demonstrate that very minor amino acid substitutions have a significant effect on the dissociation constant and give some insight into why the dissociation constants for site III and IV in TnC are 100-fold smaller than those for sites I and II. The results suggest that the differences in coordinating ligands between sites II and III have very little effect on Ca2+ affinity and that the noncoordinating residues in the site II loop are responsible for the low affinity of site II compared to the high affinity of site III in TnC.
[NMR paper] NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural di
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J Biol Chem. 2005 Jun 17;280(24):22582-9
Authors: Howard MJ, Smales CM
The non-enzymatic reaction between reducing sugars and long-lived proteins in vivo results in the formation of glycation and advanced glycation end products, which alter the properties of proteins including charge,...
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[NMR paper] NMR probing of protein-protein interactions using reporter ligands and affinity tags.
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J Am Chem Soc. 2004 Feb 18;126(6):1636-7
Authors: Ludwiczek ML, Baminger B, Konrat R
A novel method is proposed for the detection and quantification of protein-protein interactions in solution. In this approach, one protein binding partner is tagged with a ligand binding domain, and protein-protein interaction is monitored via changes in the NMR relaxation...
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[NMR paper] Pressure-dependent changes in the structure of the melittin alpha-helix determined by
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J Biomol NMR. 2001 Feb;19(2):115-24
Authors: Iwadate M, Asakura T, Dubovskii PV, Yamada H, Akasaka K, Williamson MP
A novel method is described, which uses changes in NMR chemical shifts to characterise the structural change in a protein with pressure. Melittin in methanol is a small alpha-helical protein, and its chemical shifts change linearly...
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[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
Biochemistry. 1997 Nov 4;36(44):13657-66
Authors: Wang G, Sparrow JT, Cushley RJ
The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....
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[NMR paper] PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, w
PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study.
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Biochemistry. 1995 Sep 12;34(36):11617-24
Authors: Chupin V, Killian JA, Breg J, de Jongh HH, Boelens R, Kaptein R, de Kruijff B
Proteins that are destined for export out of the cytoplasm of Escherichia coli cells are...
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[NMR paper] Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening
Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening and dimerization monitored by nmr chemical shifts.
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Biopolymers. 1994 May;34(5):647-61
Authors: Jiménez MA, Carreño C, Andreu D, Blanco FJ, Herranz J, Rico M, Nieto JL
The solution structure of a peptide fragment corresponding to the 38-59 region of porcine phospholipase A2 has been investigated using CD,...
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[NMR paper] Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening
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Biopolymers. 1994 May;34(5):647-61
Authors: Jiménez MA, Carreño C, Andreu D, Blanco FJ, Herranz J, Rico M, Nieto JL
The solution structure of a peptide fragment corresponding to the 38-59 region of porcine phospholipase A2 has been investigated using CD,...
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08-22-2010 03:33 AM
[NMR paper] Probing the relationship between alpha-helix formation and calcium affinity in tropon
Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.
Related Articles Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.
Biochemistry. 1991 Aug 27;30(34):8339-47
Authors: Shaw GS, Hodges RS, Sykes BD
Three 34-residue peptides corresponding to the high-affinity calcium-binding site...
Probing the relationship between alpha-helix formation and calcium affinity in tropon
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