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 *

86 related articles for article (PubMed ID: 25974529)

  • 1. Pairwise amino acid secondary structural propensities.
    Chemmama IE; Chapagain PP; Gerstman BS
    Phys Rev E Stat Nonlin Soft Matter Phys; 2015 Apr; 91(4):042709. PubMed ID: 25974529
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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]  

  • 3. 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]  

  • 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. PreSSAPro: a software for the prediction of secondary structure by amino acid properties.
    Costantini S; Colonna G; Facchiano AM
    Comput Biol Chem; 2007 Oct; 31(5-6):389-92. PubMed ID: 17888742
    [TBL] [Abstract][Full Text] [Related]  

  • 6. 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]  

  • 7. Contact pair dynamics during folding of two small proteins: chicken villin head piece and the Alzheimer protein beta-amyloid.
    Mukherjee A; Bagchi B
    J Chem Phys; 2004 Jan; 120(3):1602-12. PubMed ID: 15268287
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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]  

  • 9. Structural basis for the varying propensities of different amino acids to adopt the collagen conformation.
    Raman SS; Gopalakrishnan R; Wade RC; Subramanian V
    J Phys Chem B; 2011 Mar; 115(11):2593-607. PubMed ID: 21361324
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Amino acid propensities are position-dependent throughout the length of alpha-helices.
    Engel DE; DeGrado WF
    J Mol Biol; 2004 Apr; 337(5):1195-205. PubMed ID: 15046987
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Molecular dynamics simulations of peptides and proteins with a continuum electrostatic model based on screened Coulomb potentials.
    Hassan SA; Mehler EL; Zhang D; Weinstein H
    Proteins; 2003 Apr; 51(1):109-25. PubMed ID: 12596268
    [TBL] [Abstract][Full Text] [Related]  

  • 12. A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure.
    Malkov SN; Zivković MV; Beljanski MV; Hall MB; Zarić SD
    J Mol Model; 2008 Aug; 14(8):769-75. PubMed ID: 18504624
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Amino acid pair- and triplet-wise groupings in the interior of α-helical segments in proteins.
    de Sousa MM; Munteanu CR; Pazos A; Fonseca NA; Camacho R; Magalhães AL
    J Theor Biol; 2011 Feb; 271(1):136-44. PubMed ID: 21130100
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Intrinsic disorder in the Protein Data Bank.
    Le Gall T; Romero PR; Cortese MS; Uversky VN; Dunker AK
    J Biomol Struct Dyn; 2007 Feb; 24(4):325-42. PubMed ID: 17206849
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Statistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequence.
    Pahlke D; Freund C; Leitner D; Labudde D
    BMC Struct Biol; 2005 Apr; 5():8. PubMed ID: 15804350
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. I. Solvent accessibility classes.
    Wako H; Blundell TL
    J Mol Biol; 1994 May; 238(5):682-92. PubMed ID: 8182743
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Tri-peptide reference structures for the calculation of relative solvent accessible surface area in protein amino acid residues.
    Topham CM; Smith JC
    Comput Biol Chem; 2015 Feb; 54():33-43. PubMed ID: 25544680
    [TBL] [Abstract][Full Text] [Related]  

  • 18. A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank.
    Bastolla U; Porto M; Roman HE; Vendruscolo M
    BMC Evol Biol; 2006 May; 6():43. PubMed ID: 16737532
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Nature versus design: the conformational propensities of D-amino acids and the importance of side chain chirality.
    Towse CL; Hopping G; Vulovic I; Daggett V
    Protein Eng Des Sel; 2014 Nov; 27(11):447-55. PubMed ID: 25233851
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Use of conserved key amino acid positions to morph protein folds.
    Reddy BV; Li WW; Bourne PE
    Biopolymers; 2002 Jul; 64(3):139-45. PubMed ID: 12012349
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 5.