Thanks to X-ray crystallography, we now have detailed structural information on a number of proteins. When this is combined with results from enzyme kinetics and from studies of inhibitors, detailed mechanisms can sometimes be proposed for enzyme action. This does not, however, mean that enzyme structure and function is now understood. We cannot yet predict the shape of a protein from its amino acid sequence, or the subtle conformational effects caused by the mutation of one amino acid into another. More structural information is required before proteins can be designed for particular novel functions. NMR spectroscopy can provide some of the vital statistics.
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Latvian Inst Organ Synth, Lab Phys Organ Chem, Riga, LatviaLatvian Inst Organ Synth, Lab Phys Organ Chem, Riga, Latvia
Kitoka, Kristine
Skrabana, Rostislav
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Slovak Acad Sci, Inst Neuroimmunol, Bratislava, Slovakia
AXON Neurosci R&D Serv SE, Bratislava, SlovakiaLatvian Inst Organ Synth, Lab Phys Organ Chem, Riga, Latvia
Skrabana, Rostislav
Gasparik, Norbert
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Masaryk Univ, Cent European Inst Technol, Brno, Czech Republic
Masaryk Univ, Fac Sci, Natl Ctr Biomol Res, Brno, Czech RepublicLatvian Inst Organ Synth, Lab Phys Organ Chem, Riga, Latvia
Gasparik, Norbert
Hritz, Jozef
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Masaryk Univ, Cent European Inst Technol, Brno, Czech Republic
Masaryk Univ, Fac Sci, Dept Chem, Brno, Czech RepublicLatvian Inst Organ Synth, Lab Phys Organ Chem, Riga, Latvia
Hritz, Jozef
Jaudzems, Kristaps
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Latvian Inst Organ Synth, Lab Phys Organ Chem, Riga, Latvia
Univ Latvia, Fac Chem, Riga, LatviaLatvian Inst Organ Synth, Lab Phys Organ Chem, Riga, Latvia