Characterization of soluble artificial proteins with random sequences.
FEBS Lett
; 421(2): 147-51, 1998 Jan 09.
Article
en En
| MEDLINE
| ID: mdl-9468296
ABSTRACT
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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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
Tipo de estudio:
Clinical_trials
Idioma:
En
Revista:
FEBS Lett
Año:
1998
Tipo del documento:
Article
País de afiliación:
Japón