Detail of "7423-96-3"

Reference

Evaluating the Potential of Fluorinated Tyrosines as Spectroscopic Probes of Local Protein Environments: A UV Resonance Raman Study

Evaluating the Potential of Fluorinated Tyrosines as Spectroscopic Probes of Local Protein Environments: A UV Resonance Raman Study. Reid, Philip J.; Loftus, Christine; Beeson, Craig C. (Department of Chemistry, University of Washington, Seattle, WA 98195, USA). Biochemistry, 42(8), 2441-2448 (English) 2003 American Chemical Society. CODEN: BICHAW. ISSN: 0006-2960. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) Section cross-reference(s): 34 UV resonance Raman (UVRR) studies designed to test the utility of fluorinated tyrosines as spectroscopic probes of the local environment are presented. Specifically, resonance Raman spectra of 2-fluoro-L-tyrosine and 3-fluoro-L-tyrosine (3-Yf) obtained with 229 nm excitation are reported. In contrast to the modest environmental dependence of the tyrosine resonance Raman spectrum, the spectrum of 3-Yf is found to be extremely dependent on the hydrogen bonding strength of the surrounding environment. Preliminary ab initio studies suggest that this behavior is due to normal modes having dominant contributions from the C-OH and C-F internal coordinates. Hydrogen bonding to the solvent perturbs the internal coordinate energetics and/or couplings, thereby altering the character of the normal modes and the corresponding transition frequencies and/or intensities. In addn. to the solvent studies, 3-Yf is site specifically incorporated into the influenza hemagglutinin (HA) 100-107 peptide which binds to the Fv fragment of the 17/9 anti-HA(98-108) peptide antibody. These studies demonstrate that the spectrum of 3-Yf can be monitored in the presence of native tyrosine. In summary, the studies presented here demonstrate that 3-Yf holds exceptional promise as a probe of the protein environment. 7423-96-3 which is the cas registry number of one of substances is just one of reagents here. .

Structural and Spectral Response of Aequorea victoria Green Fluorescent Proteins to Chromophore Fluorination

Structural and Spectral Response of Aequorea victoria Green Fluorescent Proteins to Chromophore Fluorination. Pal, Prajna P.; Bae, Jae Hyun; Azim, M. Kamran; Hess, Petra; Friedrich, Rainer; Huber, Robert; Moroder, Luis; Budisa, Nediljko ( Max-Planck-Institut fuer Biochemie, Martinsried 82152, Germany). Biochemistry, 44(10), 3663-3672 (English) 2005 American Chemical Society. CODEN: BICHAW. ISSN: 0006-2960. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 75 Global replacements of tyrosine by 2- and 3-fluorotyrosine in "enhanced green" and "enhanced yellow" mutants of Aequorea victoria green fluorescent proteins (avGFPs) provided protein variants with novel biophys. properties. While crystallog. and modeled structures of these proteins are indistinguishable from those of their native counterparts (i.e., they are perfectly isomorphous), there are considerable differences in their spectroscopic properties. The fluorine being an integral part of the avGFP chromophore induces changes in the titrn. curves, variations in the intensity of the absorbance and fluorescence, and spectral shifts in the emission maxima. Furthermore, targeted fluorination in close proximity to the fluorinated chromophore yielded addnl. variants with considerably enhanced spectral changes. These unique spectral properties are intrinsic features of the fluorinated avGFPs, in the context of the rigid chromophore-microenvironment interactions. The availability of the isomorpohous crystal structures of fluorinated avGFPs allowed mapping of novel, unusual interaction distances created by the presence of fluorine atoms. In addn., fluorine atoms in the ortho position of the chromophore tyrosyl moiety exhibit a single conformation, while in the meta position two conformer states were obsd. in the cryst. state. Such global replacements in chromophores of avGFPs and similar proteins result in "at.Some chemicals with cas registry numbers like 7423-96-3 are also used. mutations" (i.e., H ? F replacements) in the structures, offering unprecedented opportunities to understand and manipulate the relationships between protein structure and spectroscopic properties. .