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Structural studies of phospholipase A2, in the presence of micelles, and investigations into molecular properties of lipids indicate that the mechanism of interracial activation of lipolytic enzymes may be far more complex than presently supposed at present.
The determination of the crystal structure of the ribonuclease inhibitor-ribonuclease A complex provides exciting new insight on how the leucine-rich repeat allows a single molecule to get around the problem of inhibiting an entire family of enzymes.
A defined, spontaneous protein folding defect can act as a common link between lung and liver diseases associated with the Z type of plasma α1-antitrypsin deficiency.
Examination of FK506, cyclosporin and rapamycin has revealed that the surface loops involved in molecular recognition may need to be rigid as well as hydrophobic.
