DIVERSIFIED SEQUENCES OF PEPTIDE EPITOPE FOR SAME-RNA RECOGNITION

被引：17

作者：

KIM, S ^{[1
]}

DEPOUPLANA, LR ^{[1
]}

SCHIMMEL, P ^{[1
]}

机构：

[1] MIT,DEPT BIOL,CAMBRIDGE,MA 02139

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 21期

关键词：

AMINOACYL-TRANSFER RNA SYNTHETASE; METHIONYL-TRANSFER RNA SYNTHETASE; ESCHERICHIA-COLI; COMBINATORIAL SEQUENCE LIBRARY; INVERSE PROTEIN FOLDING;

D O I：

10.1073/pnas.90.21.10046

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We replaced an essential RNA-binding, 30-amino acid helix-loop in an Escherichia coli tRNA synthetase with an inactive and simplified ''generic'' sequence having 23 of the 30 amino acids as alanine and serine. Wild-type residues were restored in random combinations to generate a library with a sequence complexity of about 1.9 x 10(7). Active molecules were obtained by genetic selection at a frequency of almost-equal-to 1% and contained variants with as many as 11 alanine/serine replacements and a total of 17 alanine/serine residues. These variants have activities which are thermodynamically competitive with that of the native protein and therefore are functionally and, most likely, conformationally equivalent.

引用

页码：10046 / 10050

页数：5

共 27 条

[1]

BARKER DG, 1982, EUR J BIOCHEM, V127, P449

[2] A METHOD TO IDENTIFY PROTEIN SEQUENCES THAT FOLD INTO A KNOWN 3-DIMENSIONAL STRUCTURE [J].