Related ArticlesConformational analysis of a mitochondrial presequence derived from the F1-ATPase beta-subunit by CD and NMR spectroscopy.
Biochim Biophys Acta. 1992 Sep 4;1159(1):81-93
Authors: Bruch MD, Hoyt DW
Previous studies on mitochondrial targeting presequences have indicated that formation of an amphiphillic helix may be required for efficient targeting of the precursor protein into mitochondria, but the structural details are not well understood. We have used CD and NMR spectroscopy to characterize in detail the structure of a synthetic peptide corresponding to the presequence for the beta-subunit of F1-ATPase, a mitochondrial matrix protein. Although this peptide is essentially unstructured in water, alpha-helix formation is induced when the peptide is placed in structure-promoting environments, such as SDS micelles or aqueous trifluoroethanol (TFE). In 50% TFE (by volume), the peptide is in dynamic equilibrium between random coil and alpha-helical conformations, with a significant population of alpha-helix throughout the entire peptide. The helix is somewhat more stable in the N-terminal part of the presequence (residues 4-10), and this result is consistent with the structure proposed previously for the presequence of another mitochondrial matrix protein, yeast cytochrome oxidase subunit IV. Addition of increasing amounts of TFE causes the alpha-helical content to increase even further, and the TFE titration data for the presequence peptide of the F1-ATPase beta-subunit are not consistent with a single, cooperative transition from random coil to alpha-helix. There is evidence that helix formation is initiated in two different regions of the peptide. This result helps to explain the redundancy of the targeting information contained in the presequence for the F1-ATPase beta-subunit.
[NMR paper] NMR-based determination of the binding epitope and conformational analysis of MUC-1 g
NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3.
Related Articles NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3.
Eur J Biochem. 2002 Mar;269(5):1444-55
Authors: Möller H, Serttas N, Paulsen H, Burchell JM, Taylor-Papadimitriou J,
Mucin glycoproteins on breast cancer cells carry shortened...
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[NMR paper] Analysis of error propagation from NMR-derived internuclear distances into molecular
Analysis of error propagation from NMR-derived internuclear distances into molecular structure of cyclo-pro-gly.
Related Articles Analysis of error propagation from NMR-derived internuclear distances into molecular structure of cyclo-pro-gly.
J Magn Reson. 1998 Dec;135(2):454-65
Authors: Dzakula Z, Jurani? , DeRider ML, Westler WM, Macura S, Markley JL
Analytical expressions have been derived that translate uncertainties in distance constraints (obtained from NMR investigations) into uncertainties in atom positions in the maximum likelihood...
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[NMR paper] Protein structural analysis from solid-state NMR-derived orientational constraints.
Protein structural analysis from solid-state NMR-derived orientational constraints.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Protein structural analysis from solid-state NMR-derived orientational constraints.
Biophys J. 1997 May;72(5):2342-8
Authors: Quine JR, Brenneman MT, Cross TA
High-resolution orientational constraints from solid-state NMR...
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[NMR paper] Protein structural analysis from solid-state NMR-derived orientational constraints.
Protein structural analysis from solid-state NMR-derived orientational constraints.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Protein structural analysis from solid-state NMR-derived orientational constraints.
Biophys J. 1997 May;72(5):2342-8
Authors: Quine JR, Brenneman MT, Cross TA
High-resolution orientational constraints from solid-state NMR...
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[NMR paper] Synthesis and conformational analysis by 1H NMR and restrained molecular dynamics sim
Synthesis and conformational analysis by 1H NMR and restrained molecular dynamics simulations of the cyclic decapeptide
Related Articles Synthesis and conformational analysis by 1H NMR and restrained molecular dynamics simulations of the cyclic decapeptide
J Comput Aided Mol Des. 1996 Jun;10(3):213-32
Authors: Buono RA, Kucharczyk N, Neuenschwander M, Kemmink J, Hwang LY, Fauchère JL, Venanzi CA
The design of enzyme mimics with therapeutic and industrial applications has interested both experimental and computational chemists for several...
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[NMR paper] Molecular dynamics-derived conformation and intramolecular interaction analysis of th
Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
Related Articles Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
...
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[NMR paper] Conformational analysis of protein structures derived from NMR data.
Conformational analysis of protein structures derived from NMR data.
Related Articles Conformational analysis of protein structures derived from NMR data.
Proteins. 1993 Nov;17(3):232-51
Authors: MacArthur MW, Thornton JM
A study is presented of the conformational characteristics of NMR-derived protein structures in the Protein Data Bank compared to X-ray structures. Both ensemble and energy-minimized average structures are analyzed. We have addressed the problem using the methods developed for crystal structures by examining the distribution...
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[NMR paper] Conformational preferences of synthetic peptides derived from the immunodominant site
Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR.
Related Articles Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR.
Biochemistry. 1990 Aug 28;29(34):7828-37
Authors: Dyson HJ, Satterthwait AC, Lerner RA, Wright PE
Proton nuclear magnetic resonance and ultraviolet circular dichroism spectroscopy have been used to probe the conformational...