Towards label-free and site-specific probing of the local pH in proteins: pH-dependent deep UV Raman spectra of histidine and tyrosine
Autor(en): | Broeermann, Andreas Steinhoff, Heinz-Juergen Schluecker, Sebastian |
Stichwörter: | AMINO-ACIDS; Aromatic amino acids; BIOPHYSICAL CHEMISTRY; Chemistry; Chemistry, Physical; DYNAMICS; H-BONDS; LIVING CELLS; Microenvironment; PEPTIDE RECOGNITION; RESIDUES; Resonance Raman spectroscopy; SENSORY RHODOPSIN II; SPECTROSCOPY; WATER | Erscheinungsdatum: | 2014 | Herausgeber: | ELSEVIER SCIENCE BV | Journal: | JOURNAL OF MOLECULAR STRUCTURE | Volumen: | 1073 | Ausgabe: | SI | Startseite: | 77 | Seitenende: | 81 | Zusammenfassung: | The site-specific pH is an experimental probe for assessing models of structural folding and function of a protein as well as protein protein and protein ligand interactions. It can be determined by various techniques such as NMR, FT-IR, fluorescence and EPR spectroscopy. The latter require the use of external labels, i.e., employ pH-dependent dyes and spin labels, respectively. In this contribution, we outline an approach to a label-free and site-specific method for determining the local pH using deep ultraviolet resonance Raman (UVRR) spectroscopic fingerprints of the aromatic amino acids histidine and tyrosine in combination with a robust algorithm that determines the pH value using three UVRR reference spectra and without prior knowledge of the pK(a). (C) 2014 Elsevier B.V. All rights reserved. |
ISSN: | 00222860 | DOI: | 10.1016/j.molstruc.2014.03.053 |
Show full item record