Labeling proteins via hole burning of their aromatic amino acids: pressure tuning spectroscopy of BPTI.
We demonstrate hole burning on a protein by using an intrinsic aromatic amino acid as a probe. The protein is bovine pancreatic trypsin inhibitor (BPTI), the labeled amino acid is tyrosine. Only one of the four tyrosines could be burned. As an application we present pressure tuning experiments from which the local compressibility around the burned tyrosine probe is determined.
Stübner
Markus
M
Physik Department E14--Lehrstuhl für Physik Weihenstephan, Technische Universität München, Vottinger Strasse 40, 85350 Freising, Germany.
Hecht
Christoph
C
Friedrich
Josef
J
D024322:Amino Acids, Aromatic / Q000737:chemistry; D007611:Aprotinin / Q000032:analysis / Q000737:chemistry*; D011312:Pressure; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D012680:Sensitivity and Specificity; D013056:Spectrophotometry, Ultraviolet / Q000379:methods*; D013194:Staining and Labeling / Q000379:methods*; D014443:Tyrosine / Q000737:chemistry*
D024322:Amino Acids, Aromatic; D011506:Proteins; D014443:Tyrosine; D007611:Aprotinin