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Volumn 129, Issue 17, 2007, Pages 5419-5429

The origins of femtomolar protein-ligand binding: Hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding site

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS; LIGANDS; MOLECULAR DYNAMICS; QUANTUM THEORY; UREA;

EID: 34247897078     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja066950n     Document Type: Article
Times cited : (156)

References (128)
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    • (2004) Gaussian 03, revision , Issue.C.02
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    • University of California: San Francisco, CA
    • Case, D. A.; et al. Amber 8; University of California: San Francisco, CA, 2004.
    • (2004) Amber 8
    • Case, D.A.1
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    • Oxford University Press: New York
    • Scheiner, S. Hydrogen Bonding; Oxford University Press: New York, 1997.
    • (1997) Hydrogen Bonding
    • Scheiner, S.1
  • 119
    • 34247865353 scopus 로고    scopus 로고
    • The dipole for the bicyclic urea in the streptavidin model binding site is derived by subtracting the dipole vector contributions of the surrounding hydrogen-bonding residues from the total dipole moment
    • The dipole for the bicyclic urea in the streptavidin model binding site is derived by subtracting the dipole vector contributions of the surrounding hydrogen-bonding residues from the total dipole moment.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.