BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

262 related articles for article (PubMed ID: 6548264)

  • 1. Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect.
    Richmond TJ
    J Mol Biol; 1984 Sep; 178(1):63-89. PubMed ID: 6548264
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Hydrophobic regions on protein surfaces: definition based on hydration shell structure and a quick method for their computation.
    Eisenhaber F; Argos P
    Protein Eng; 1996 Dec; 9(12):1121-33. PubMed ID: 9010925
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature.
    Tsodikov OV; Record MT; Sergeev YV
    J Comput Chem; 2002 Apr; 23(6):600-9. PubMed ID: 11939594
    [TBL] [Abstract][Full Text] [Related]  

  • 4. FACTS: Fast analytical continuum treatment of solvation.
    Haberthür U; Caflisch A
    J Comput Chem; 2008 Apr; 29(5):701-15. PubMed ID: 17918282
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Quantification of the hydrophobic interaction by simulations of the aggregation of small hydrophobic solutes in water.
    Raschke TM; Tsai J; Levitt M
    Proc Natl Acad Sci U S A; 2001 May; 98(11):5965-9. PubMed ID: 11353861
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Discrimination between native and intentionally misfolded conformations of proteins: ES/IS, a new method for calculating conformational free energy that uses both dynamics simulations with an explicit solvent and an implicit solvent continuum model.
    Vorobjev YN; Almagro JC; Hermans J
    Proteins; 1998 Sep; 32(4):399-413. PubMed ID: 9726412
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Hydrophobic regions on protein surfaces. Derivation of the solvation energy from their area distribution in crystallographic protein structures.
    Eisenhaber F
    Protein Sci; 1996 Aug; 5(8):1676-86. PubMed ID: 8844856
    [TBL] [Abstract][Full Text] [Related]  

  • 8. The importance of excluded solvent volume effects in computing hydration free energies.
    Yang PK; Lim C
    J Phys Chem B; 2008 Nov; 112(47):14863-8. PubMed ID: 18956834
    [TBL] [Abstract][Full Text] [Related]  

  • 9. A set of van der Waals and coulombic radii of protein atoms for molecular and solvent-accessible surface calculation, packing evaluation, and docking.
    Li AJ; Nussinov R
    Proteins; 1998 Jul; 32(1):111-27. PubMed ID: 9672047
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Surface area included in energy refinement of proteins. A comparative study on atomic solvation parameters.
    von Freyberg B; Richmond TJ; Braun W
    J Mol Biol; 1993 Sep; 233(2):275-92. PubMed ID: 7690855
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Universal solvation model based on solute electron density and on a continuum model of the solvent defined by the bulk dielectric constant and atomic surface tensions.
    Marenich AV; Cramer CJ; Truhlar DG
    J Phys Chem B; 2009 May; 113(18):6378-96. PubMed ID: 19366259
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Efficient approximate all-atom solvent accessible surface area method parameterized for folded and denatured protein conformations.
    Guvench O; Brooks CL
    J Comput Chem; 2004 Jun; 25(8):1005-14. PubMed ID: 15067676
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Analysis of accessible surface of residues in proteins.
    Lins L; Thomas A; Brasseur R
    Protein Sci; 2003 Jul; 12(7):1406-17. PubMed ID: 12824487
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Simple physics-based analytical formulas for the potentials of mean force for the interaction of amino acid side chains in water. 1. Approximate expression for the free energy of hydrophobic association based on a Gaussian-overlap model.
    Makowski M; Liwo A; Scheraga HA
    J Phys Chem B; 2007 Mar; 111(11):2910-6. PubMed ID: 17388416
    [TBL] [Abstract][Full Text] [Related]  

  • 15. A hydrophobic spine stabilizes a surface-exposed α-helix according to analysis of the solvent-accessible surface area.
    Liou YF; Huang HL; Ho SY
    BMC Bioinformatics; 2016 Dec; 17(Suppl 19):503. PubMed ID: 28155647
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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]  

  • 17. The SGB/NP hydration free energy model based on the surface generalized born solvent reaction field and novel nonpolar hydration free energy estimators.
    Gallicchio E; Zhang LY; Levy RM
    J Comput Chem; 2002 Apr; 23(5):517-29. PubMed ID: 11948578
    [TBL] [Abstract][Full Text] [Related]  

  • 18. SAMPL5: 3D-RISM partition coefficient calculations with partial molar volume corrections and solute conformational sampling.
    Luchko T; Blinov N; Limon GC; Joyce KP; Kovalenko A
    J Comput Aided Mol Des; 2016 Nov; 30(11):1115-1127. PubMed ID: 27585474
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Excluded volume approximation to protein-solvent interaction. The solvent contact model.
    Colonna-Cesari F; Sander C
    Biophys J; 1990 May; 57(5):1103-7. PubMed ID: 2340343
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Rapid refinement of protein interfaces incorporating solvation: application to the docking problem.
    Jackson RM; Gabb HA; Sternberg MJ
    J Mol Biol; 1998 Feb; 276(1):265-85. PubMed ID: 9514726
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 14.