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1 ~ away from the zinc atom. The hydroxamate nitrogen is The protein catalyst pNB esterasehas been the shown to be protonated. One oxygen atom of the subject of two orthogonal directed-evolution sulfone group appears to serve as a hydrogen bond screens, one for organic activity and another for acceptor for the amide nitrogen of a Ieucine residue thermostability, resulting in proteins with a 100-fold on beta-strand 4. These studies demonstrate that increase in activity and a 17°C increase in stability, MMP inhibitor selectivity is principally determined respectively.

Figure I Structure of the hypothetical protein MJ0577 in the hyperthermophilic archaebacterium Methanococcusjanncnchii, solved at the MCE (Left) Electron-density map derived from MAD experimental phases clearly shows a bound ATP (yellow stick structure). (Right) The tertiary structure of MJ0577 is a nucleotide binding fold. The discovery of the ATP immediately narrows down the possible biochemical function of this pro- Investigators T. -W. Hung, J. Mueller- tein. -K. Kim*, H.

Menzel (Technische Universitat Munchen, Germany); and C. Heske (Berkeley Lab). Publications 1. A. , “Beyond the chemical shift: Vlbrationally resolved core-level spectra of adsorbed CO,” I%ys. Rev. Lett. 81, 1730 (1998). resolution was better than 10,000 between photon energies of 250 eV and 700 eV. 2. A. , ccVlbrational fine structure in core level photoelectron lines of adsorbed mole- The observation of vibrational fine structure in the XPS main lines of adsorbed molecules leads to a sig- cules: System dependent effects,” J.

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