Premium
Total synthesis by modern chemical ligation methods and high resolution (1.1 Å) X‐ray structure of ribonuclease A
Author(s) -
Boerema David J.,
Tereshko Valentina A.,
Kent Stephen B. H.
Publication year - 2008
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20800
Subject(s) - preprint , chemistry , rnase p , chemical ligation , resolution (logic) , ribonuclease , angstrom , native chemical ligation , nanotechnology , crystallography , chemical synthesis , computer science , biochemistry , rna , materials science , amino acid , world wide web , in vitro , gene , artificial intelligence
The total chemical synthesis of RNase A using modern chemical ligation methods is described, illustrating the significant advances that have been made in chemical protein synthesis since Gutte and Merrifield's pioneering preparation of RNase A in 1969. The identity of the synthetic product was confirmed through rigorous characterization, including the determination of the X‐ray crystal structure to 1.1 Angstrom resolution. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90:278–286, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom