532 related articles for article (PubMed ID: 7490751)
1. 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]
2. 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]
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. 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]
5. Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins.
Avbelj F
J Mol Biol; 2000 Jul; 300(5):1335-59. PubMed ID: 10903873
[TBL] [Abstract][Full Text] [Related]
6. Influence of side chain conformations on local conformational features of amino acids and implication for force field development.
Jiang F; Han W; Wu YD
J Phys Chem B; 2010 May; 114(17):5840-50. PubMed ID: 20392111
[TBL] [Abstract][Full Text] [Related]
7. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations.
Smith LJ; Bolin KA; Schwalbe H; MacArthur MW; Thornton JM; Dobson CM
J Mol Biol; 1996 Jan; 255(3):494-506. PubMed ID: 8568893
[TBL] [Abstract][Full Text] [Related]
8. Toward direct determination of conformations of protein building units from multidimensional NMR experiments VI: chemical shift analysis of his to gain 3D structure and protonation state information.
Hudáky P; Perczel A
J Comput Chem; 2005 Oct; 26(13):1307-17. PubMed ID: 15999335
[TBL] [Abstract][Full Text] [Related]
9. Side-chains in native and random coil protein conformations. Analysis of NMR coupling constants and chi1 torsion angle preferences.
West NJ; Smith LJ
J Mol Biol; 1998 Jul; 280(5):867-77. PubMed ID: 9671556
[TBL] [Abstract][Full Text] [Related]
10. Properties of polyproline II, a secondary structure element implicated in protein-protein interactions.
Cubellis MV; Caillez F; Blundell TL; Lovell SC
Proteins; 2005 Mar; 58(4):880-92. PubMed ID: 15657931
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. 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]
13. Free energy determinants of secondary structure formation: I. alpha-Helices.
Yang AS; Honig B
J Mol Biol; 1995 Sep; 252(3):351-65. PubMed ID: 7563056
[TBL] [Abstract][Full Text] [Related]
14. The beta-turn scaffold of tripeptide containing an azaphenylalanine residue.
Lee HJ; Park HM; Lee KB
Biophys Chem; 2007 Jan; 125(1):117-26. PubMed ID: 16890344
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. 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]
17. [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]
18. The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins.
Beck DA; Alonso DO; Inoyama D; Daggett V
Proc Natl Acad Sci U S A; 2008 Aug; 105(34):12259-64. PubMed ID: 18713857
[TBL] [Abstract][Full Text] [Related]
19. Influence of the environment in the conformation of alpha-helices studied by protein database search and molecular dynamics simulations.
Olivella M; Deupi X; Govaerts C; Pardo L
Biophys J; 2002 Jun; 82(6):3207-13. PubMed ID: 12023245
[TBL] [Abstract][Full Text] [Related]
20. 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; 44(28):9691-702. PubMed ID: 16008354
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
