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Journal Abstract Search

122 related items for PubMed ID: 8378312

  • 1. What determines the strength of noncovalent association of ligands to proteins in aqueous solution?
    Miyamoto S, Kollman PA.
    Proc Natl Acad Sci U S A; 1993 Sep 15; 90(18):8402-6. PubMed ID: 8378312
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  • 2. Absolute and relative binding free energy calculations of the interaction of biotin and its analogs with streptavidin using molecular dynamics/free energy perturbation approaches.
    Miyamoto S, Kollman PA.
    Proteins; 1993 Jul 15; 16(3):226-45. PubMed ID: 8346190
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  • 3. Structural origins of high-affinity biotin binding to streptavidin.
    Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR.
    Science; 1989 Jan 06; 243(4887):85-8. PubMed ID: 2911722
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  • 4. Effects of tryptophan residue fluorination on streptavidin stability and biotin-streptavidin interactions via molecular dynamics simulations.
    Panek JJ, Ward TR, Jezierska A, Novic M.
    J Mol Model; 2009 Mar 06; 15(3):257-66. PubMed ID: 19052784
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  • 5. What determines the van der Waals coefficient beta in the LIE (linear interaction energy) method to estimate binding free energies using molecular dynamics simulations?
    Wang W, Wang J, Kollman PA.
    Proteins; 1999 Feb 15; 34(3):395-402. PubMed ID: 10024025
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  • 6. Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin.
    Sano T, Cantor CR.
    Proc Natl Acad Sci U S A; 1995 Apr 11; 92(8):3180-4. PubMed ID: 7724536
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  • 7. Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site.
    Gitlin G, Bayer EA, Wilchek M.
    Biochem J; 1988 Nov 15; 256(1):279-82. PubMed ID: 3223904
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  • 11. Effect of conformational flexibility and solvation on receptor-ligand binding free energies.
    Vajda S, Weng Z, Rosenfeld R, DeLisi C.
    Biochemistry; 1994 Nov 29; 33(47):13977-88. PubMed ID: 7947806
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  • 12. Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex.
    Freitag S, Le Trong I, Chilkoti A, Klumb LA, Stayton PS, Stenkamp RE.
    J Mol Biol; 1998 May 29; 279(1):211-21. PubMed ID: 9636711
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  • 13. Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120.
    Chilkoti A, Tan PH, Stayton PS.
    Proc Natl Acad Sci U S A; 1995 Feb 28; 92(5):1754-8. PubMed ID: 7878054
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  • 14. Essentials of biorecognition: the (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction.
    Wilchek M, Bayer EA, Livnah O.
    Immunol Lett; 2006 Feb 28; 103(1):27-32. PubMed ID: 16325268
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  • 15. Temperature control of biotin binding and release with A streptavidin-poly(N-isopropylacrylamide) site-specific conjugate.
    Ding Z, Long CJ, Hayashi Y, Bulmus EV, Hoffman AS, Stayton PS.
    Bioconjug Chem; 1999 Feb 28; 10(3):395-400. PubMed ID: 10346869
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  • 16. Stable, high-affinity streptavidin monomer for protein labeling and monovalent biotin detection.
    Lim KH, Huang H, Pralle A, Park S.
    Biotechnol Bioeng; 2013 Jan 28; 110(1):57-67. PubMed ID: 22806584
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  • 17. Homogeneous noncompetitive assay of protein via Förster-resonance-energy-transfer with tryptophan residue(s) as intrinsic donor(s) and fluorescent ligand as acceptor.
    Liao F, Xie Y, Yang X, Deng P, Chen Y, Xie G, Zhu S, Liu B, Yuan H, Liao J, Zhao Y, Yu M.
    Biosens Bioelectron; 2009 Sep 15; 25(1):112-7. PubMed ID: 19586766
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  • 20. Studies on the biotin-binding sites of avidin and streptavidin. A chemically induced dynamic nuclear polarization investigation of the status of tyrosine residues.
    Gitlin G, Khait I, Bayer EA, Wilchek M, Muszkat KA.
    Biochem J; 1989 Apr 15; 259(2):493-8. PubMed ID: 2719662
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