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Exploring the Structural Impact of Unnatural Amino Acids on Protein Structure
Author(s) -
Savidge Nicole S,
Maurici Nicole,
Brewer Scott H,
PhillipsPiro Christine M
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.603.20
Subject(s) - chemistry , amino acid , protein structure , green fluorescent protein , phenylalanine , crystal structure , biochemistry , crystallography , gene
Unnatural amino acids (UAAs) have the potential to serve as effective, site‐specific reporters of local protein structure and dynamics. However, in order to act as an effective probe, the UAA needs to be minimally perturbative to the native protein structure. One potential IR probe of local environment is 4‐nitro‐L‐phenylalanine (pNO 2 F). pNO 2 F has been genetically incorporated into the model protein superfolder green fluorescent protein (sfGFP) at a solvated and partially buried site individually in order to determine the structural impact of the presence of the UAAs on the native protein structure. The IR analysis of these protein constructs in addition to the protein crystal structures will be presented. Support or Funding Information • The F&M Hackman Scholars Program and Schappell Research Fund • NIH R15 (2R15GM09330) to S.H.B/E.E.F.