Total synthesis by modern chemical ligation methods and high resolution (1.1 Å) X-ray structure of ribonuclease A

• Published in: Biopolymers 2008, Vol.90 (3), p.278-286
• Main Authors: Boerema, David J., Tereshko, Valentina A., Kent, Stephen B. H.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Catalysis; Cattle; CRYSTAL STRUCTURE; Cysteine - chemistry; Disulfides - chemistry; Hydrogen Bonding; Kinetics; MATERIALS SCIENCE; Models, Chemical; Molecular Sequence Data; native chemical ligation; Protein Conformation; Protein Folding; Protein Structure, Secondary; PROTEINS; RESOLUTION; ribonuclease A; Ribonuclease, Pancreatic - analysis; Ribonuclease, Pancreatic - chemical synthesis; Ribonuclease, Pancreatic - chemistry; Ribonuclease, Pancreatic - isolation & purification; RNA-ASE; solid phase peptide synthesis; SYNTHESIS; total chemical synthesis; Water - chemistry; X-Ray Diffraction; X-ray structure
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/bip.20800

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 [e-mail]