Thermodynamic analysis of biomolecular interactions

Current Opinion in Chemical Biology

Volumn 3, Issue 5, 1999, Pages 557-563

  Cooper, Alan ^a  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEIC ACID; PROTEIN;

ENTHALPY; ENTROPY; MOLECULAR INTERACTION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; REVIEW; THERMODYNAMICS;

EID: 0032850996     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)00008-3     Document Type: Review

References (64)

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33. •] illustrating the ongoing arguments.
34. •] illustrating the ongoing arguments.
35. •]) examining carefully the effects of mutations at protein-protein interfaces, illustrating how difficult it still is to rationalise the thermodynamics of such changes, even when detailed structural information is available. Water molecules fill available voids to optimise close packing.
36. •].
37. •].
38. •].
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62. •]) in the mechanical manipulation of single protein molecules and the way this can be used to measure directly the forces necessary for unfolding or protein-protein interaction.
63. •]) in the mechanical manipulation of single protein molecules and the way this can be used to measure directly the forces necessary for unfolding or protein-protein interaction.
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