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215 related items for PubMed ID: 22223291

  • 1. A comprehensive library of blocked dipeptides reveals intrinsic backbone conformational propensities of unfolded proteins.
    Oh KI, Lee KK, Park EK, Jung Y, Hwang GS, Cho M.
    Proteins; 2012 Apr; 80(4):977-90. PubMed ID: 22223291
    [Abstract] [Full Text] [Related]

  • 2. Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins.
    Avbelj F.
    J Mol Biol; 2000 Jul 28; 300(5):1335-59. PubMed ID: 10903873
    [Abstract] [Full Text] [Related]

  • 3. Site-selective intramolecular hydrogen-bonding interactions in phosphorylated serine and threonine dipeptides.
    Lee KK, Kim E, Joo C, Song J, Han H, Cho M.
    J Phys Chem B; 2008 Dec 25; 112(51):16782-7. PubMed ID: 19049417
    [Abstract] [Full Text] [Related]

  • 4. Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.
    Serrano L.
    J Mol Biol; 1995 Nov 24; 254(2):322-33. PubMed ID: 7490751
    [Abstract] [Full Text] [Related]

  • 5. Neighboring residue effects in terminally blocked dipeptides: implications for residual secondary structures in intrinsically unfolded/disordered proteins.
    Jung YS, Oh KI, Hwang GS, Cho M.
    Chirality; 2014 Sep 24; 26(9):443-52. PubMed ID: 24453185
    [Abstract] [Full Text] [Related]

  • 6. Intrinsic backbone preferences are fully present in blocked amino acids.
    Avbelj F, Grdadolnik SG, Grdadolnik J, Baldwin RL.
    Proc Natl Acad Sci U S A; 2006 Jan 31; 103(5):1272-7. PubMed ID: 16423894
    [Abstract] [Full Text] [Related]

  • 7. Nearest-neighbor effects and structural preferences in dipeptides are a function of the electronic properties of amino acid side-chains.
    Dwyer DS.
    Proteins; 2006 Jun 01; 63(4):939-48. PubMed ID: 16477601
    [Abstract] [Full Text] [Related]

  • 8. Conformational analysis of XA and AX dipeptides in water by electronic circular dichroism and 1H NMR spectroscopy.
    Hagarman A, Measey T, Doddasomayajula RS, Dragomir I, Eker F, Griebenow K, Schweitzer-Stenner R.
    J Phys Chem B; 2006 Apr 06; 110(13):6979-86. PubMed ID: 16571011
    [Abstract] [Full Text] [Related]

  • 9. Design of ferrocene-dipeptide bioorganometallic conjugates to induce chirality-organized structures.
    Moriuchi T, Hirao T.
    Acc Chem Res; 2010 Jul 20; 43(7):1040-51. PubMed ID: 20377253
    [Abstract] [Full Text] [Related]

  • 10. Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library.
    Jha AK, Colubri A, Zaman MH, Koide S, Sosnick TR, Freed KF.
    Biochemistry; 2005 Jul 19; 44(28):9691-702. PubMed ID: 16008354
    [Abstract] [Full Text] [Related]

  • 11. Determination of conformational preferences of dipeptides using vibrational spectroscopy.
    Grdadolnik J, Grdadolnik SG, Avbelj F.
    J Phys Chem B; 2008 Mar 06; 112(9):2712-8. PubMed ID: 18260662
    [Abstract] [Full Text] [Related]

  • 12. Azido gauche effect on the backbone conformation of β-azidoalanine peptides.
    Oh KI, Kim W, Joo C, Yoo DG, Han H, Hwang GS, Cho M.
    J Phys Chem B; 2010 Oct 14; 114(40):13021-9. PubMed ID: 20849143
    [Abstract] [Full Text] [Related]

  • 13. The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.
    Jiang F, Han W, Wu YD.
    Phys Chem Chem Phys; 2013 Mar 14; 15(10):3413-28. PubMed ID: 23385383
    [Abstract] [Full Text] [Related]

  • 14. Role of enthalpy-entropy compensation interactions in determining the conformational propensities of amino acid residues in unfolded peptides.
    Toal SE, Verbaro DJ, Schweitzer-Stenner R.
    J Phys Chem B; 2014 Feb 06; 118(5):1309-18. PubMed ID: 24423055
    [Abstract] [Full Text] [Related]

  • 15. Dissecting the stability of a beta-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the beta-turn and beta-strand contributions to folding.
    Griffiths-Jones SR, Maynard AJ, Searle MS.
    J Mol Biol; 1999 Oct 08; 292(5):1051-69. PubMed ID: 10512702
    [Abstract] [Full Text] [Related]

  • 16. Secondary structures of short peptide chains in the gas phase: double resonance spectroscopy of protected dipeptides.
    Chin W, Dognon JP, Canuel C, Piuzzi F, Dimicoli I, Mons M, Compagnon I, von Helden G, Meijer G.
    J Chem Phys; 2005 Feb 01; 122(5):54317. PubMed ID: 15740332
    [Abstract] [Full Text] [Related]

  • 17. Diproline templates as folding nuclei in designed peptides. Conformational analysis of synthetic peptide helices containing amino terminal Pro-Pro segments.
    Rai R, Aravinda S, Kanagarajadurai K, Raghothama S, Shamala N, Balaram P.
    J Am Chem Soc; 2006 Jun 21; 128(24):7916-28. PubMed ID: 16771506
    [Abstract] [Full Text] [Related]

  • 18. Folding of aminosuccinyl peptides: thermodynamic data from temperature dependent circular dichroism measurements.
    Capasso S, Mazzarella L, Zagari A.
    Chirality; 1995 Jun 21; 7(8):605-9. PubMed ID: 8593254
    [Abstract] [Full Text] [Related]

  • 19. Direct calculations of vibrational absorption and circular dichroism spectra of alanine dipeptide analog in water: quantum mechanical/molecular mechanical molecular dynamics simulations.
    Yang S, Cho M.
    J Chem Phys; 2009 Oct 07; 131(13):135102. PubMed ID: 19814574
    [Abstract] [Full Text] [Related]

  • 20. De novo design, synthesis and solution conformational study of two didehydroundecapeptides: effect of nature and number of amino acids interspersed between ΔPhe residues.
    Dutta MG, Mathur P, Chauhan VS.
    J Pept Sci; 2011 Dec 07; 17(12):783-90. PubMed ID: 21997956
    [Abstract] [Full Text] [Related]

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