Ultraviolet resonance Raman spectroscopy of folded and unfolded states of an integral membrane protein.

doi:10.1021/jp800772j

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Article

Ultraviolet resonance Raman spectroscopy of folded and unfolded states of an integral membrane protein.

The journal of physical chemistry. B - 7 Aug 2008

Sanchez Katheryn M, Neary Tiffany J, Kim Judy E

Abstract excerpt

The vibrational structure of native anchoring tryptophan (Trp) and tyrosine residues in an integral membrane protein, bacterial outer membrane protein A (OmpA), have been investigated using UV resonance Raman (UVRR) spectroscopy for the first time. Spectra of native OmpA, a single-Trp mutant, and a Trp-less mutant were recorded in folded and unfolded states, and reveal significant changes in tryptophan structure...

Topics

Bacterial Outer Membrane Proteins
Membrane Proteins
Models, Molecular
Mutation
Protein Folding
Protein Structure, Tertiary
Spectrum Analysis, Raman

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Open in PubMed

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PMID: 18588328
DOI: 10.1021/jp800772j

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