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Journal Abstract Search


531 related items for PubMed ID: 17279623

  • 21. Triaspartate: a model system for conformationally flexible DDD motifs in proteins.
    Duitch L, Toal S, Measey TJ, Schweitzer-Stenner R.
    J Phys Chem B; 2012 May 03; 116(17):5160-71. PubMed ID: 22435395
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  • 22. Conformational preferences of a short Aib/Ala-based water-soluble peptide as a function of temperature.
    Banerjee R, Chattopadhyay S, Basu G.
    Proteins; 2009 Jul 03; 76(1):184-200. PubMed ID: 19137603
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  • 23. Predictions of secondary structure using statistical analyses of electronic and vibrational circular dichroism and Fourier transform infrared spectra of proteins in H2O.
    Baumruk V, Pancoska P, Keiderling TA.
    J Mol Biol; 1996 Jun 21; 259(4):774-91. PubMed ID: 8683582
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  • 24. Vibrational circular dichroism and IR spectral analysis as a test of theoretical conformational modeling for a cyclic hexapeptide.
    Bour P, Kim J, Kapitan J, Hammer RP, Huang R, Wu L, Keiderling TA.
    Chirality; 2008 Nov 21; 20(10):1104-19. PubMed ID: 18506832
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  • 25. Inter-residue coupling and equilibrium unfolding of PPII helical peptides. Vibrational spectra enhanced with (13)C isotopic labeling.
    Chi H, Lakhani A, Roy A, Nakaema M, Keiderling TA.
    J Phys Chem B; 2010 Oct 07; 114(39):12744-53. PubMed ID: 20831224
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  • 26. Simulated IR, isotropic and anisotropic Raman, and vibrational circular dichroism amide I band profiles of stacked β-sheets.
    Schweitzer-Stenner R.
    J Phys Chem B; 2012 Apr 12; 116(14):4141-53. PubMed ID: 22390232
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  • 27. Vibrational circular dichroism as a probe of fibrillogenesis: the origin of the anomalous intensity enhancement of amyloid-like fibrils.
    Measey TJ, Schweitzer-Stenner R.
    J Am Chem Soc; 2011 Feb 02; 133(4):1066-76. PubMed ID: 21186804
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  • 33. Uncoupled peptide bond vibrations in alpha-helical and polyproline II conformations of polyalanine peptides.
    Mikhonin AV, Asher SA.
    J Phys Chem B; 2005 Feb 24; 109(7):3047-52. PubMed ID: 16851319
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  • 34. Circular dichroism eigenspectra of polyproline II and β-strand conformers of trialanine in water: Singular value decomposition analysis.
    Oh KI, Lee KK, Park EK, Yoo DG, Hwang GS, Cho M.
    Chirality; 2010 Feb 24; 22 Suppl 1():E186-201. PubMed ID: 21038390
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  • 40. The preferred conformation of the tripeptide Ala-Phe-Ala in water is an inverse gamma-turn: implications for protein folding and drug design.
    Motta A, Reches M, Pappalardo L, Andreotti G, Gazit E.
    Biochemistry; 2005 Nov 01; 44(43):14170-8. PubMed ID: 16245933
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