FEBS Letters · 1998 · 37 citations · 18 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProtein FoldingEnzyme FunctionGlobular ProteinsMacromolecular AssemblyProtein CharacterizationProtein ChemistryProtein StructureEsterase ActivityMolten Globule StatesPeptide Secondary StructureProtein CrystallographyProtein Self-assemblyProtein Structural EvolutionProtein Structure DeterminationRate Constant Determination
The structural and catalytic properties of two soluble random proteins, RP3-42 and RP3-45, of 141 amino acid residues were investigated. Although no marked secondary structure was detected by CD spectrum, sedimentation equilibrium and small-angle X-ray scattering studies showed that they form an oligomeric structure and are as compact as the molten globule. The random proteins have low but distinct esterase activity; the values of the second-order rate constant for the hydrolysis of p-nitrophenol were 0.78 and 1.39 M(-1) s(-1) for RP3-42 and RP3-45, respectively. The differences in the properties of the random and the native proteins are discussed from the evolutionary point of view.
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<i>Small-Angle Scattering of X-Rays</i>
A. Guinier, G. Fournet, C. B. Walker et al. · Physics Today · 1956 · 4.3K citations