Deep-UV Resonance Raman Analysis of theRhodobacter capsulatusCytochromebc1Complex Reveals a Potential Marker for the Transmembrane Peptide Backbone

Biochemistry ◽  
2011 ◽  
Vol 50 (30) ◽  
pp. 6531-6538 ◽  
Author(s):  
Christopher M. Halsey ◽  
Olayinka O. Oshokoya ◽  
Renee D. Jiji ◽  
Jason W. Cooley
Keyword(s):  
Resonance Raman ◽  
Peptide Backbone ◽  
Raman Analysis ◽  
Potential Marker ◽  
Uv Resonance Raman ◽  
Deep Uv

Simultaneous Observation of Peptide Backbone Lipid Solvation and α-Helical Structure by Deep-UV Resonance Raman Spectroscopy

ChemBioChem ◽  
2011 ◽  
Vol 12 (14) ◽  
pp. 2125-2128 ◽  
Author(s):  
Christopher M. Halsey ◽  
Jian Xiong ◽  
Olayinka O. Oshokoya ◽  
Jeanette A. Johnson ◽  
Sandip Shinde ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Helical Structure ◽  
Simultaneous Observation ◽  
Peptide Backbone ◽  
Uv Resonance Raman ◽  
Uv Resonance Raman Spectroscopy ◽  
Deep Uv

Ultrasensitivein situTracing of the Alkaloid Dioncophylline A in the Tropical LianaTriphyophyllum peltatumby Applying Deep-UV Resonance Raman Microscopy

2007 ◽  
Vol 79 (3) ◽  
pp. 986-993 ◽  
Author(s):  
Torsten Frosch ◽  
Michael Schmitt ◽  
Torsten Noll ◽  
Gerhard Bringmann ◽  
Karla Schenzel ◽  
...  
Keyword(s):  
Resonance Raman ◽  
Raman Microscopy ◽  
Uv Resonance Raman ◽  
Deep Uv

scholarly journals Deep-UV Resonance Raman Spectral Properties of Membrane Proteins

2016 ◽  
Vol 110 (3) ◽  
pp. 394a
Author(s):  
Anahita Zare ◽  
Michael Eagleburger ◽  
Mia C. Brown ◽  
Christopher Halsey ◽  
Carol Roach ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Spectral Properties ◽  
Resonance Raman ◽  
Uv Resonance Raman ◽  
Deep Uv ◽  
Raman Spectral

scholarly journals Monitoring membrane protein structural changes and interactions via deep UV resonance Raman spectroscopy

2015 ◽  
Author(s):  
◽  
Mia C. Brown
Keyword(s):  
Membrane Proteins ◽  
Structural Changes ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
The Body ◽  
Intramembrane Proteolysis ◽  
Parkinson’S Diseases ◽  
Uv Resonance Raman ◽  
Uv Resonance Raman Spectroscopy ◽  
Deep Uv

Membrane proteins perform a variety of functions within our cells. They transport nutrients and waste across the lipid barrier, transmit signals from one part of the body to another, and run our immune system. However, despite their ubiquitous and vital presence in all organisms, relatively little is known about this class of proteins compared to their soluble counterparts. Intramembrane proteolysis is a process involving membrane proteins that occurs in all biological organisms and has garnered particular interest due to its involvement in various disease pathologies, such as Alzheimer's and Parkinson's Diseases. In this work I have set out to use deep UV resonance Raman (DUVRR) spectroscopy to characterize structural and environmental transitions of proteins and applied the results to studies involving intramembrane proteolysis in an effort to better understand the key concepts behind it.

scholarly journals Correlation of TrpGly and GlyTrp Rotamer Structure with W7 and W10 UV Resonance Raman Modes and Fluorescence Emission Shifts

2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Azaria Solomon Eisenberg ◽  
Laura J. Juszczak
Keyword(s):  
Stark Effect ◽  
Resonance Raman ◽  
Fluorescence Emission ◽  
High Energy ◽  
Appreciable Amount ◽  
Peptide Backbone ◽  
Band Ratio ◽  
Uv Resonance Raman ◽  
Raman Modes ◽  
Discrete Values

Tryptophyl glycine (TrpGly) and glycyl tryptophan (GlyTrp) dipeptides at pH 5.5 and pH 9.3 show a pattern of fluorescence emission shifts with the TrpGly zwitterion emission solely blue shifted. This pattern is matched by shifts in the UV resonance Raman (UVRR) W10 band position and the W7 Fermi doublet band ratio. Ab initio calculations show that the 1340 cm−1 band of the W7 doublet is composed of three modes, two of which determine the W7 band ratios for the dipeptides. Molecular dynamics simulations show that the dipeptides take on two conformations: one with the peptide backbone extended; one with the backbone curled over the indole. The dihedral angle critical to these conformations is χ1 and takes on three discrete values. Only the TrpGly zwitterion spends an appreciable amount of time in the extended backbone conformation as this is stabilized by two hydrogen bonds with the terminal amine cation. According to a Stark effect model, a positive charge near the pyrrole keeps the 1La transition at high energy, limiting fluorescence emission red shift, as observed for the TrpGly zwitterion. The hydrogen bond stabilized backbone provides a rationale for the Cmethylene-Cα-Ccarbonyl W10 symmetric stretch that is unique to the TrpGly zwitterion.

Sign in / Sign up

Export Citation Format

Share Document