Soft X-ray Spectromicroscopy of Protein Interactions with Phase-Segregated Polymer Surfaces

2012 ◽  
pp. 731-760
Author(s):  
Adam P. Hitchcock ◽  
Bonnie O. Leung ◽  
John L. Brash ◽  
Andreas Scholl ◽  
Andrew Doran
Keyword(s):  
Protein Interactions ◽  
Polymer Surfaces ◽  
X Ray

scholarly journals Chemical Mapping of Polymer Microstructure Using Soft X-ray Spectromicroscopy

2005 ◽  
Vol 58 (6) ◽  
pp. 423 ◽  
Author(s):  
Adam P. Hitchcock ◽  
Harald D. H. Stöver ◽  
Lisa M. Croll ◽  
Ronald F. Childs
Keyword(s):  
Protein Interactions ◽  
Polymer Surfaces ◽  
Chemical Mapping ◽  
Polymer Microstructure ◽  
X Ray ◽  
Potential Control ◽  
Sample Data ◽  
Scanning Transmission ◽  
X Ray Absorption ◽  
Conducting Polymer Films

Recently, synchrotron-based soft X-ray spectromicroscopy techniques have been applied to studies of polymer microstructure at the ~50 nm spatial scale. Functional group based chemical speciation and quantitative mapping is provided by near edge X-ray absorption fine structure spectral (NEXAFS) contrast. The techniques, sample data, and analysis methods of scanning transmission X-ray microscopy (STXM) and X-ray photoemission electron microscopy (X-PEEM) are outlined. The capabilities of STXM are illustrated by results from recent studies of (a) controlled release microcapsules and microspheres, (b) microcapsules being developed for gene therapy applications, (c) conducting polymer films studied in the presence of electrolyte and under potential control, and (d) studies of protein interactions with patterned polymer surfaces. In the latter area, the capabilities of STXM and X-PEEM are compared directly.

Exploiting Soft and Hard X-Ray Absorption Spectroscopy to Characterize Metallodrug/Protein Interactions: the Binding of [trans-RuCl4(Im)(dimethylsulfoxide)][ImH] (Im = imidazole) to Bovine Serum Albumin

2008 ◽  
Vol 47 (19) ◽  
pp. 8629-8634 ◽  
Author(s):  
Isabella Ascone ◽  
Luigi Messori ◽  
Angela Casini ◽  
Chiara Gabbiani ◽  
Antonella Balerna ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Absorption Spectroscopy ◽  
Protein Interactions ◽  
Bovine Serum ◽  
X Ray ◽  
X Ray Absorption

scholarly journals Homogeneously N-glycosylated proteins derived from the GlycoDelete HEK293 cell line enable diffraction-quality crystallogenesis

2020 ◽  
Vol 76 (12) ◽  
pp. 1244-1255
Author(s):  
Sandra Kozak ◽  
Yehudi Bloch ◽  
Steven De Munck ◽  
Aleksandra Mikula ◽  
Isabel Bento ◽  
...  
Keyword(s):  
Cell Line ◽  
Protein Interactions ◽  
Successful Implementation ◽  
Structural Studies ◽  
Protein Fragments ◽  
X Ray ◽  
X Ray Crystallography ◽  
Cryo Electron Microscopy ◽  
Acid Protein ◽  
Stimulating Factor

Structural studies of glycoproteins and their complexes provide critical insights into their roles in normal physiology and disease. Most glycoproteins contain N-linked glycosylation, a key post-translation modification that critically affects protein folding and stability and the binding kinetics underlying protein interactions. However, N-linked glycosylation is often an impediment to yielding homogeneous protein preparations for structure determination by X-ray crystallography or other methods. In particular, obtaining diffraction-quality crystals of such proteins and their complexes often requires modification of both the type of glycosylation patterns and their extent. Here, we demonstrate the benefits of producing target glycoproteins in the GlycoDelete human embryonic kidney 293 cell line that has been engineered to produce N-glycans as short glycan stumps comprising N-acetylglucosamine, galactose and sialic acid. Protein fragments of human Down syndrome cell-adhesion molecule and colony-stimulating factor 1 receptor were obtained from the GlycoDelete cell line for crystallization. The ensuing reduction in the extent and complexity of N-glycosylation in both protein molecules compared with alternative glycoengineering approaches enabled their productive deployment in structural studies by X-ray crystallography. Furthermore, a third successful implementation of the GlycoDelete technology focusing on murine IL-12B is shown to lead to N-glycosylation featuring an immature glycan in diffraction-quality crystals. It is proposed that the GlycoDelete cell line could serve as a valuable go-to option for the production of homogeneous glycoproteins and their complexes for structural studies by X-ray crystallography and cryo-electron microscopy.

scholarly journals X-Ray Absorption Studies of Ti/Polymer and Cr/Polymer Interfaces

1993 ◽  
Vol 304 ◽  
Author(s):  
R. L. Opila ◽  
K. Konstadinidis ◽  
A. O. Ibidunni ◽  
A. J. Davenport ◽  
H. S. Isaacs
Keyword(s):  
Absorption Spectroscopy ◽  
Polymer Surfaces ◽  
Polymer Interfaces ◽  
Final Reaction Product ◽  
X Ray ◽  
Metal Atoms ◽  
Absorption Studies ◽  
In Situ Heating ◽  
X Ray Absorption

AbstractThe interface formed between metals, Ti and Cr, and polymers, epoxy and triazine, have been studied, nondestructively, using x-ray absorption spectroscopy. The metals were sputtered onto the polymer surfaces. Titanium reacts extensively, up to Ti thicknesses of 100 Å while Cr remains primarily metallic. In situ heating at 200°C increases the extent of reaction for both metals. Heating has a greater effect on metal/epoxy interfaces than metal/triazine. Titanium and Cr were ion implanted into the polymer in order to determine the interactions of isolated metal atoms with the polymer. Titanium and Cr appear to form oxides as the final reaction product, and the Ti is tetrahedrally coordinated.

Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacterium glutamicum

2009 ◽  
Vol 390 (8) ◽  
Author(s):  
Reinhard Krämer ◽  
Christine Ziegler
Keyword(s):  
Amino Acid ◽  
Corynebacterium Glutamicum ◽  
Protein Interactions ◽  
Regulation Mechanism ◽  
Protein Protein Interactions ◽  
Molecular Switching ◽  
X Ray ◽  
X Ray Crystallography ◽  
Terminal Domain ◽  
Domain Reorientation

Abstract Activation of the osmoregulated trimeric betaine transporter BetP from Corynebacterium glutamicum was shown to depend mainly on the correct folding and integrity of its 55 amino acid long, partly α-helical C-terminal domain. Reorientation of the three C-terminal domains in the BetP trimer indicates different lipid-protein and protein-protein interactions of the C-terminal domain during osmoregulation. A regulation mechanism is suggested where this domain switches the transporter from the inactive to the active state. Interpretation of recently obtained electron and X-ray crystallography data of BetP led to a structure-function based model of C-terminal molecular switching involved in osmoregulation.

Model Investigations for Vanadium-Protein Interactions: Synthesis and X-ray Structures of mer-[VOCl3(Hpycan)] and [VOCl2(CH3CN)(Hpycan)] {Hpycan = N-(2-Nitrophenyl)pyridine-2-carboxamide}

1994 ◽  
Vol 33 (5) ◽  
pp. 845-846 ◽  
Author(s):  
Themistoklis A. Kabanos ◽  
Anastasios D. Keramidas ◽  
Aggelos Papaioannou ◽  
Aris Terzis
Keyword(s):  
Protein Interactions ◽  
X Ray

X-ray photoelectron spectroscopy studies of polymer surfaces, 4?further studies of the chromic acid etching of low density polyethylene

1980 ◽  
Vol 2 (3) ◽  
pp. 107-114 ◽  
Author(s):  
D. Briggs ◽  
V. J. I. Zichy ◽  
D. M. Brewis ◽  
J. Comyn ◽  
R. H. Dahm ◽  
...  
Keyword(s):  
Photoelectron Spectroscopy ◽  
Chromic Acid ◽  
Polymer Surfaces ◽  
Low Density Polyethylene ◽  
Acid Etching ◽  
Low Density ◽  
X Ray ◽  
Spectroscopy Studies

Exploring Chromophore−Protein Interactions in Fluorescent Protein cmFP512 fromCerianthus membranaceus:  X-ray Structure Analysis and Optical Spectroscopy†

Biochemistry ◽  
2006 ◽  
Vol 45 (43) ◽  
pp. 12942-12953 ◽  
Author(s):  
Karin Nienhaus ◽  
Fabiana Renzi ◽  
Beatrice Vallone ◽  
Jörg Wiedenmann ◽  
G. Ulrich Nienhaus
Keyword(s):  
Optical Spectroscopy ◽  
Structure Analysis ◽  
Protein Interactions ◽  
Fluorescent Protein ◽  
X Ray

Metal Deposition on Laser Modified Teflon Surfaces

1995 ◽  
Vol 385 ◽  
Author(s):  
Stefan Lätsch ◽  
Hiroyuki Hiraoka ◽  
Joachim Bargon
Keyword(s):  
Raman Spectroscopy ◽  
Photoelectron Spectroscopy ◽  
Deposition Process ◽  
Metal Deposition ◽  
Polymer Surfaces ◽  
Good Adhesion ◽  
X Ray ◽  
Micro Raman Spectroscopy ◽  
Polymer Adhesion ◽  
Secondary Ion

ABSTRACTCu, Ni, and Au were deposited with defined patterns and good adhesion by electroless plating, e-beam evaporation, and sputtering onto Teflon (polytetrafluoroethylene, PTFE), Teflon ET (PTFE-co-ethylene), Teflon FEP (PTFE-co-hexafluoropropylene) and Teflon PFA (PTFE-coperfluoroalkoxy vinyl ether) surfaces. The polymers had been irradiated in a tetramethyl – ammonium hydoxide solution (TMAH) by a Nd:YAG laser at 266 rim and by an excimer laser at 248 nrm prior to the metal deposition process. Both, the treated and virgin polymer surfaces were characterized by x-ray photoelectron spectroscopy (XPS), secondary ion mass spectroscopy (SIMS) and Micro-Raman spectroscopy. The increased metal to polymer adhesion at the interface was found to be due to chemical changes and is in the order Ni > Cu ≅ Au.

scholarly journals The Importance of Protein-Protein Interactions on the pH-Induced Conformational Changes of Bovine Serum Albumin: A Small Angle X-Ray Scattering Study

2010 ◽  
Vol 98 (3) ◽  
pp. 630a ◽  
Author(s):  
Leandro R.S. Barbosa ◽  
Maria Grazia Ortore ◽  
Francesco Spinozzi ◽  
Paolo Mariani ◽  
Sigrid Bernstorff ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Small Angle ◽  
Bovine Serum ◽  
Protein Protein Interactions ◽  
X Ray ◽  
X Ray Scattering ◽  
Scattering Study
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