Monitoring Membrane Protein Structural Changes and Interactions Via Deep UV Resonance Raman Spectroscopy

Monitoring Membrane Protein Structural Changes and Interactions Via Deep UV Resonance Raman Spectroscopy
Author: Mia C. Brown
Publisher:
Total Pages: 94
Release: 2015
Genre:
ISBN:

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. 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 proteases and their substrates. DUVRR has been used extensively to observe protein secondary structure. This work contains the results of three main studies I have conducted during my graduate career. In the first I show results from the first experiment to look simultaneously at both secondary and tertiary structure as a protein transitions from a molten globule to ordered state. In the second study tracks the structural and environmental changes of a small peptide as it transitions from a soluble, disordered state through two membrane-bound, structurally ordered states. I was then able to apply the findings of these experiments to study intramembrane proteolysis, wherein I describe substrate characteristics and their interactions with proteases.

Methods in Protein Structure and Stability Analysis: Vibrational spectroscopy

Methods in Protein Structure and Stability Analysis: Vibrational spectroscopy
Author: Vladimir N. Uversky
Publisher: Nova Publishers
Total Pages: 326
Release: 2007
Genre: Science
ISBN: 9781600217036

Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.

Deep UV Resonance Raman Spectral Properties of Alpha Helical Membrane Proteins

Deep UV Resonance Raman Spectral Properties of Alpha Helical Membrane Proteins
Author: Anahita Zare
Publisher:
Total Pages: 109
Release: 2017
Genre:
ISBN:

Membrane protein function and structure determination is vital for pharmaceutical development and disease prevention. Despite the various methods of protein structure elucidation in use, a need still exists for techniques that are of adequate resolution, rapid, inexpensive, and compatible with the membrane environment of these proteins. Deep UV resonance Raman (dUVRR) spectroscopy is an emerging structurally sensitive spectroscopic technique for analyzing membrane protein structure. The backbone amide modes are resonance enhanced in dUVRR spectra while the membrane's lipid features are not, resulting in strong membrane protein spectral features in near native environments. In order to better define dUVRR spectral features of membrane proteins, a series of model helical peptides, poly(LA)7, were designed. By substituting select residues of the transmembrane region of poly(LA)7, the propensity of helical structure within a membrane has also been studied. Using these model membrane peptides in increasingly dehydrated environments (aqueous, surfactant, and bilayer), hydration depended changes in the spectra are characterized.

Ultraviolet Spectroscopy of Proteins

Ultraviolet Spectroscopy of Proteins
Author: Alexander P. Demchenko
Publisher: Springer Science & Business Media
Total Pages: 323
Release: 2013-11-11
Genre: Science
ISBN: 3642708471

The aim of this book is to give a comprehensive description of the basic methods used in the ultraviolet spectroscopy of proteins, to discuss new trends and development of these methods, and to analyze their different applications in the study of various aspects of protein structure and dynamics. Ultraviolet spectroscopy is one of the oldest and most popular methods in the field of biochemistry and molecular biophysics. At present, it is difficult to imagine the biochemical laboratory without a recording spectrophotometer or spectrofluorimeter. There are several hundreds of publications directly devoted to protein ultraviolet spectroscopy and in a great number of studies UV spectroscopic methods are used for the structural analysis of different proteins. Meanwhile a unified description of the theoretical basis of the methods, experimental techniques, data analysis, and generalization of results obtained in solving the specific problems of protein structure are lacking. There are three reasons for which a monograph on ultraviolet spectroscopy is needed today. Firstly, there has been significant growth in facilities of experimental technique, its precision, and versatility associated with computer data analysts. This new technique is available to a wide circle of scientists engaged in the field of protein research. Most of them are not spectroscopists and, thus, there is a need for a conceivable and precise source of information on how to use this method and what kind of data it should provide.