These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

240 related articles for article (PubMed ID: 7731949)

  • 1. Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.
    Muñoz V; Serrano L
    Proteins; 1994 Dec; 20(4):301-11. PubMed ID: 7731949
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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; 254(2):322-33. PubMed ID: 7490751
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.
    Griffiths-Jones SR; Sharman GJ; Maynard AJ; Searle MS
    J Mol Biol; 1998 Dec; 284(5):1597-609. PubMed ID: 9878373
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Amino acid propensities for secondary structures are influenced by the protein structural class.
    Costantini S; Colonna G; Facchiano AM
    Biochem Biophys Res Commun; 2006 Apr; 342(2):441-51. PubMed ID: 16487481
    [TBL] [Abstract][Full Text] [Related]  

  • 5. [A turning point in the knowledge of the structure-function-activity relations of elastin].
    Alix AJ
    J Soc Biol; 2001; 195(2):181-93. PubMed ID: 11727705
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Position dependence of non-polar amino acid intrinsic helical propensities.
    Petukhov M; Muñoz V; Yumoto N; Yoshikawa S; Serrano L
    J Mol Biol; 1998 Apr; 278(1):279-89. PubMed ID: 9571050
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Comprehensive analysis of the helix-X-helix motif in soluble proteins.
    Deville J; Rey J; Chabbert M
    Proteins; 2008 Jul; 72(1):115-35. PubMed ID: 18214950
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Free energies of amino acid side-chain rotamers in alpha-helices, beta-sheets and alpha-helix N-caps.
    Stapley BJ; Doig AJ
    J Mol Biol; 1997 Sep; 272(3):456-64. PubMed ID: 9325103
    [TBL] [Abstract][Full Text] [Related]  

  • 9. An integrated approach to the analysis and modeling of protein sequences and structures. III. A comparative study of sequence conservation in protein structural families using multiple structural alignments.
    Yang AS; Honig B
    J Mol Biol; 2000 Aug; 301(3):691-711. PubMed ID: 10966778
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Intrinsic propensities of amino acid residues in GxG peptides inferred from amide I' band profiles and NMR scalar coupling constants.
    Hagarman A; Measey TJ; Mathieu D; Schwalbe H; Schweitzer-Stenner R
    J Am Chem Soc; 2010 Jan; 132(2):540-51. PubMed ID: 20014772
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Thermodynamic beta-sheet propensities measured using a zinc-finger host peptide.
    Kim CA; Berg JM
    Nature; 1993 Mar; 362(6417):267-70. PubMed ID: 8459852
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Conformational similarity indices between different residues in proteins and alpha-helix propensities.
    Pal D; Chakrabarti P
    J Biomol Struct Dyn; 2000 Oct; 18(2):273-80. PubMed ID: 11089648
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures.
    Swindells MB; MacArthur MW; Thornton JM
    Nat Struct Biol; 1995 Jul; 2(7):596-603. PubMed ID: 7664128
    [TBL] [Abstract][Full Text] [Related]  

  • 14. NdPASA: a novel pairwise protein sequence alignment algorithm that incorporates neighbor-dependent amino acid propensities.
    Wang J; Feng JA
    Proteins; 2005 Feb; 58(3):628-37. PubMed ID: 15616964
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Residual structure in unfolded proteins revealed by Raman optical activity.
    Wilson G; Hecht L; Barron LD
    Biochemistry; 1996 Sep; 35(38):12518-25. PubMed ID: 8823188
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Protein folding kinetics provides a context-independent assessment of beta-strand propensity in the Fyn SH3 domain.
    Zarrine-Afsar A; Dahesh S; Davidson AR
    J Mol Biol; 2007 Oct; 373(3):764-74. PubMed ID: 17850820
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Interactions between a helical residue and tertiary structures: helix propensities in small peptides and in native proteins.
    Qian H; Chan SI
    J Mol Biol; 1996 Aug; 261(2):279-88. PubMed ID: 8757294
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Protein folds: towards understanding folding from inspection of native structures.
    Thornton JM; Jones DT; MacArthur MW; Orengo CM; Swindells MB
    Philos Trans R Soc Lond B Biol Sci; 1995 Apr; 348(1323):71-9. PubMed ID: 7770489
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. II. Secondary structures.
    Wako H; Blundell TL
    J Mol Biol; 1994 May; 238(5):693-708. PubMed ID: 8182744
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Local propensities and statistical potentials of backbone dihedral angles in proteins.
    Betancourt MR; Skolnick J
    J Mol Biol; 2004 Sep; 342(2):635-49. PubMed ID: 15327961
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 12.