Search

Your search keyword '"Burban, David J."' showing total 7 results
Start Over Author "Burban, David J."
7 results on '"Burban, David J."'

2. Proximity‐Enabled Protein Crosslinking through Genetically Encoding Haloalkane Unnatural Amino Acids

Author

Xiang, Zheng, Lacey, Vanessa K, Ren, Haiyan, Xu, Jing, Burban, David J, Jennings, Patricia A, and Wang, Lei

Subjects
Chemical Sciences, Generic health relevance, Alkanes, Amino Acids, Amino Acyl-tRNA Synthetases, Cysteine, Cysteine Endopeptidases, Halogens, Protein Binding, Protein Engineering, RNA, Transfer, Recombinant Fusion Proteins, protein crosslinking, protein engineering, proximity-enabled reactivity, tRNA, unnatural amino acids, Organic Chemistry, Chemical sciences
Abstract

The selective generation of covalent bonds between and within proteins would provide new avenues for studying protein function and engineering proteins with new properties. New covalent bonds were genetically introduced into proteins by enabling an unnatural amino acid (Uaa) to selectively react with a proximal natural residue. This proximity-enabled bioreactivity was expanded to a series of haloalkane Uaas. Orthogonal tRNA/synthetase pairs were evolved to incorporate these Uaas, which only form a covalent thioether bond with cysteine when positioned in close proximity. By using the Uaa and cysteine, spontaneous covalent bond formation was demonstrated between an affibody and its substrate Z protein, thereby leading to irreversible binding, and within the affibody to increase its thermostability. This strategy of proximity-enabled protein crosslinking (PEPC) may be generally expanded to target different natural amino acids, thus providing diversity and flexibility in covalent bond formation for protein research and protein engineering.

Published
2014

7. Proximity-enabled protein crosslinking through genetically encoding haloalkane unnatural amino acids.

Author

Xiang Z, Lacey VK, Ren H, Xu J, Burban DJ, Jennings PA, and Wang L

Subjects
Amino Acids chemistry, Amino Acyl-tRNA Synthetases metabolism, Cysteine chemistry, Cysteine metabolism, Cysteine Endopeptidases chemistry, Cysteine Endopeptidases metabolism, Protein Binding, Protein Engineering, RNA, Transfer metabolism, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins metabolism, Alkanes chemistry, Amino Acids metabolism, Halogens chemistry
Abstract

The selective generation of covalent bonds between and within proteins would provide new avenues for studying protein function and engineering proteins with new properties. New covalent bonds were genetically introduced into proteins by enabling an unnatural amino acid (Uaa) to selectively react with a proximal natural residue. This proximity-enabled bioreactivity was expanded to a series of haloalkane Uaas. Orthogonal tRNA/synthetase pairs were evolved to incorporate these Uaas, which only form a covalent thioether bond with cysteine when positioned in close proximity. By using the Uaa and cysteine, spontaneous covalent bond formation was demonstrated between an affibody and its substrate Z protein, thereby leading to irreversible binding, and within the affibody to increase its thermostability. This strategy of proximity-enabled protein crosslinking (PEPC) may be generally expanded to target different natural amino acids, thus providing diversity and flexibility in covalent bond formation for protein research and protein engineering., (Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Published
2014
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results