کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1356369 | 981112 | 2006 | 11 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Total chemical synthesis of the B1 domain of protein L from Peptostreptococcus magnus Total chemical synthesis of the B1 domain of protein L from Peptostreptococcus magnus](/preview/png/1356369.png)
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.
Journal: Bioorganic Chemistry - Volume 34, Issue 3, June 2006, Pages 131–141