Total chemical synthesis of the B1 domain of protein L from Peptostreptococcus magnus.
Reported here is a native chemical ligation strategy for the total chemical synthesis of the B1 domain of protein L. A synthetic construct of this 76 amino acid protein domain was prepared by the chemoselective ligation of two unprotected polypeptide fragments, one containing an N-terminal cysteine residue and one containing a C-terminal thioester moiety. The polypeptide fragments utilized in the ligation reaction were readily prepared by stepwise solid phase peptide synthesis (SPPS) methods for Boc-chemistry. The milligram quantities of protein required for conventional biophysical studies were readily accessible using the synthetic protocol described here. The folding properties of the synthetic protein L construct were also determined and found to be very similar to those of a similar wild-type protein L constructs prepared by recombinant-DNA methods. This work facilitates future unnatural amino acid mutagenesis experiments on this model protein system to further dissect the molecular basis of its folding and stability.
Duke Scholars
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Related Subject Headings
- Time Factors
- Thermodynamics
- Peptostreptococcus
- Organic Chemistry
- Molecular Sequence Data
- Kinetics
- Bacterial Proteins
- Amino Acid Sequence
- 3405 Organic chemistry
- 3404 Medicinal and biomolecular chemistry
Citation
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Issue
Start / End Page
Related Subject Headings
- Time Factors
- Thermodynamics
- Peptostreptococcus
- Organic Chemistry
- Molecular Sequence Data
- Kinetics
- Bacterial Proteins
- Amino Acid Sequence
- 3405 Organic chemistry
- 3404 Medicinal and biomolecular chemistry