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Characterization of soluble artificial proteins with random sequences
Author(s) -
Yamauchi Asao,
Yomo Tetsuya,
Tanaka Fumihiro,
Prijambada Irfan D,
Ohhashi Seiji,
Yamamoto Keizo,
Shima Yasufumi,
Ogasahara Kyoko,
Yutani Katsuhide,
Kataoka Mikio,
Urabe Itaru
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01552-4
Subject(s) - esterase , hydrolysis , molten globule , protein secondary structure , chemistry , characterization (materials science) , small angle x ray scattering , sedimentation equilibrium , biochemistry , crystallography , enzyme , materials science , scattering , physics , nanotechnology , optics
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.