Biophysical EPR Studies Applied to Membrane Proteins

Sahu, Indra D.; Lorigan, Gary A.

doi:10.4172/2161-0398.1000188

Cited by 22 publications

(24 citation statements)

References 76 publications

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“…Under experimental conditions, these motions can be isolated from the EPR spectrum. The inverse linewidth of the central line of the EPR spectrum provides a measure of relative mobility [ 22 , 25 , 51 , 56 ]. A plot of the inverse linewidth mobility against the amino acid sequence can produce a periodic data profile, which can be used to predict the local secondary structure of the proteins and peptides [ 8 , 22 , 51 , 57 ].…”

Section: Application Of Sdsl Epr Techniques For Studying Membrane mentioning

confidence: 99%

“…EPR spectroscopy can answer pertinent structural and dynamic questions related to both solution and membrane bound proteins that are very challenging to be obtained by traditional biophysical methods [ 21 – 24 ]. CW-EPR spectroscopy of spin labeled molecules reveals structural and dynamic information about the motion of the nitroxide side-chain, solvent accessibility, solvent polarity, and intra- or intermolecular distances between two nitroxides or a single nitroxide and another paramagnetic center in the system [ 3 , 8 , 15 , 22 , 25 ]. The lineshape analysis of the EPR data for a series of spin labeled protein sequences can probe the structural properties of the protein at backbone level spatial resolution [ 26 – 29 ].…”

Section: Introductionmentioning

confidence: 99%

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Site-Directed Spin Labeling EPR for Studying Membrane Proteins

Sahu

Lorigan

2018

BioMed Research International

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Site-directed spin labeling (SDSL) in combination with electron paramagnetic resonance (EPR) spectroscopy is a rapidly expanding powerful biophysical technique to study the structural and dynamic properties of membrane proteins in a native environment. Membrane proteins are responsible for performing important functions in a wide variety of complicated biological systems that are responsible for the survival of living organisms. In this review, a brief introduction of the most popular SDSL EPR techniques and illustrations of recent applications for studying pertinent structural and dynamic properties on membrane proteins will be discussed.

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Section: Application Of Sdsl Epr Techniques For Studying Membrane mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Site-Directed Spin Labeling EPR for Studying Membrane Proteins

Sahu

Lorigan

2018

BioMed Research International

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“…δ corresponds to the central linewidth, whose inverse value is proportional to the mobility. Adapted from Dyszy et al (2013) with permission a broad range of local and collective molecular motions of proteins and membranes and have greatly contributed to the success of ESR in protein-membrane studies (Borbat et al 2001;Jeschke et al 2004;McHaourab et al 2011;Sahu and Lorigan 2015;Smirnova and Smirnov 2015).…”

Section: Spin Labeling Electron Spin Resonance (Esr)mentioning

confidence: 99%

The two sides of a lipid-protein story

2016

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Protein-membrane interactions play essential roles in a variety of cell functions such as signaling, membrane trafficking, and transport. Membrane-recruited cytosolic proteins that interact transiently and interfacially with lipid bilayers perform several of those functions. Experimental techniques capable of probing changes on the structural dynamics of this weak association are surprisingly limited. Among such techniques, electron spin resonance (ESR) has the enormous advantage of providing valuable local information from both membrane and protein perspectives by using intrinsic paramagnetic probes in metalloproteins or by attaching nitroxide spin labels to proteins and lipids. In this review, we discuss the power of ESR to unravel relevant structural and functional details of lipid-peripheral membrane protein interactions with special emphasis on local changes of specific regions of the protein and/or the lipids. First, we show how ESR can be used to investigate the direct interaction between a protein and a particular lipid, illustrating the case of lipid binding into a hydrophobic pocket of chlorocatechol 1,2-dioxygenase, a non-heme iron enzyme responsible for catabolism of aromatic compounds that are industrially released in the environment. In the second case, we show the effects of GPI-anchored tissue-nonspecific alkaline phosphatase, a protein that plays a crucial role in skeletal mineralization, and on the ordering and dynamics of lipid acyl chains. Then, switching to the protein perspective, we analyze the interaction with model membranes of the brain fatty acid binding protein, the major actor in the reversible binding and transport of hydrophobic ligands such as long-chain, saturated, or unsaturated fatty acids. Finally, we conclude by discussing how both lipid and protein views can be associated to address a common question regarding the molecular mechanism by which dihydroorotate dehydrogenase, an essential enzyme for the de novo synthesis of pyrimidine nucleotides, and how it fishes out membrane-embedded quinones to perform its function.

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“…The 6 issues of volume 5 of the Journal have published 34 articles, i.e., 7 editorials, 3 reviews, 21 research articles, 2 commentaries, and 1 conference proceeding. The research and review articles have covered a diversity of topics, ranging from self-organizing ionogels that may be used for production of soft materials with tunable properties [3] and ion-membrane interactions [4] to the biosynthesis of the fragrance of rose [5], DNA-protein interactions [6], and electron paramagnetic resonance (EPR) of membrane proteins [7].…”

mentioning

confidence: 99%

“…Finally, the review by Sahu and Lorigan [7] summarizes the achievements in the field of membrane protein structure and function, including site-specific structural characterization, obtained by EPR. The advantages of EPR, such as its high sensitivity, independence of protein size, versatility and relative ease of use, as well as the range of applications and the specific structural and dynamics information obtained are highlighted.…”

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confidence: 99%

The Journal of Physical Chemistry and Biophysics in a Turbulent World of Ever-Increasing Scientific Output

Tatulian

2016

J Phys Chem Biophys

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We live in a world of databases. We are flooded with information. Is it good or bad? It's certainly a good thing that comes with challenges. It is like a cloud with a silver lining, and the latter is real bright and luminous. Any information about atoms, molecules, supramolecular assemblies is just a few clicks away, something the mid-and even late-20 th century researchers could not even dream of. For example, you can attain the sequence and properties, and in most cases the structure, of any protein in less than a minute. Moreover, physical and chemical details of atoms and molecules such as energy levels, transitions, thermodynamics, various kinds of electronic, vibrational, and magnetic resonance spectra, are easily available from multiple databases, such as the 69 Standard Reference Databases offered by the National Institute of Standards and Technology. On the other hand, it's not easy to keep pace with the fiercely mounting scientific and technology information. Reaxys reports properties of ~ 2.2 million inorganic and organometallic compounds, PubChem offers around 160 million chemical compounds, 60 million chemical structures, and 1 million biological assays [1]. Along with over 100 million DNA and protein sequences involving ~ 260,000 species that are available through the National Center for Biotechnology Information, over 115,000 macromolecular structures deposited in the Protein Data Bank, the amount of information simply becomes incomprehensible. Oftentimes we feel like we can't see the trees because of the forest.

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Biophysical EPR Studies Applied to Membrane Proteins

Cited by 22 publications

References 76 publications

Site-Directed Spin Labeling EPR for Studying Membrane Proteins

Site-Directed Spin Labeling EPR for Studying Membrane Proteins

The two sides of a lipid-protein story

The Journal of Physical Chemistry and Biophysics in a Turbulent World of Ever-Increasing Scientific Output

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