Technology for Formation of Hybrid Microfluidic Biosensor Systems for Label-Free Fluorimetric Express Detection of Protein Structures based on Molecular Recognition

The development and comparative study of technologies for manufacturing elements of hybrid biosensor systems intended for express biomedical analysis has been carried out. The technological process included the formation of the relief of microfluidic channels, chemical modification of their working surface, deposition of solid-state phosphor layers, sealing of the system, installation of inlet ports and packaging.

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Chemical binding of pyrrolidinyl peptide nucleic acid ( acpcPNA‐T9 ) probe with AuNPs toward label‐free monitoring of miRNA ‐21: A novel biosensing platform for biomedical analysis and POC diagnostics

Journal of Molecular Recognition ◽

10.1002/jmr.2893 ◽

2021 ◽

Author(s):

Nazanin Fathi ◽

Arezoo Saadati ◽

Mohammad Hasanzadeh ◽

Mohammad Samiei

Keyword(s):

Nucleic Acid ◽

Peptide Nucleic Acid ◽

Label Free ◽

Biomedical Analysis ◽

Chemical Binding

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Europium (III) complexes with new N-donor ligand: A comparative study in solid state and solution

Polyhedron ◽

10.1016/j.poly.2013.04.012 ◽

2013 ◽

Vol 57 ◽

pp. 30-38 ◽

Cited By ~ 20

Author(s):

Fabio Piccinelli ◽

Andrea Melchior ◽

Adolfo Speghini ◽

Magda Monari ◽

Marilena Tolazzi ◽

...

Keyword(s):

Solid State ◽

Comparative Study ◽

Donor Ligand

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A comparative study of the conformational mobility of octamethyltetrasiloxane and cyclododecane in the solid state

Polymer Bulletin ◽

10.1007/bf00958664 ◽

1984 ◽

Vol 12 (6) ◽

pp. 557-563 ◽

Cited By ~ 4

Author(s):

Detlef Emeis ◽

Hans-Joachim Cantow ◽

Martin M�ller

Keyword(s):

Solid State ◽

Comparative Study ◽

Conformational Mobility

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Neutron Fluence Measurements with Solid-State Nuclear Track Detectors: Results of a Comparative Study with Gold and Indium Foils

Nuclear Technology ◽

10.13182/nt79-a32191 ◽

1979 ◽

Vol 42 (3) ◽

pp. 343-349 ◽

Cited By ~ 1

Author(s):

A. Aframian

Keyword(s):

Solid State ◽

Comparative Study ◽

Neutron Fluence ◽

Nuclear Track Detectors

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Homologous size-extension of hybrid vanadate capsules – solid state structures, solution stability and surface deposition

Chemical Communications ◽

10.1039/c3cc48541b ◽

2014 ◽

Vol 50 (18) ◽

pp. 2265-2267 ◽

Cited By ~ 19

Author(s):

Mariyatra B. Mahimaidoss ◽

Sergey A. Krasnikov ◽

Lukas Reck ◽

Camelia I. Onet ◽

John M. Breen ◽

...

Keyword(s):

Solid State ◽

Solution Stability ◽

Surface Deposition ◽

Solid State Structures

The dimensions of hybrid vanadate capsules can be controlled through organophosphonate ligands. The solution-stability allows their deposition on the Au(111) surface giving rise to densely packed 2D assemblies.

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Protein structure by solid-state NMR spectroscopy

Quarterly Reviews of Biophysics ◽

10.1017/s0033583500004017 ◽

1987 ◽

Vol 19 (1-2) ◽

pp. 7-49 ◽

Cited By ~ 137

Author(s):

S. J. Opella ◽

P. L. Stewart ◽

K. G. Valentine

Keyword(s):

Solid State ◽

Nmr Spectroscopy ◽

Solid State Nmr ◽

Structural Information ◽

Biological Systems ◽

Genetic Regulation ◽

Protein Structures ◽

Crystalline Solid ◽

Solid State Nmr Spectroscopy ◽

Nmr Methods

The three-dimensional structures of proteins are among the most valuable contributions of biophysics to the understanding of biological systems (Dickerson & Geis, 1969; Creighton, 1983). Protein structures are utilized in the description and interpretation of a wide variety of biological phenomena, including genetic regulation, enzyme mechanisms, antibody recognition, cellular energetics, and macroscopic mechanical and structural properties of molecular assemblies. Virtually all of the information currently available about the structures of proteins at atomic resolution has been obtained from diffraction studies of single crystals of proteins (Wyckoff et al, 1985). However, recently developed NMR methods are capable of determining the structures of proteins and are now being applied to a variety of systems, including proteins in solution and other non-crystalline environments that are not amenable for X-ray diffraction studies. Solid-state NMR methods are useful for proteins that undergo limited overall reorientation by virtue of their being in the crystalline solid state or integral parts of supramolecular structures that do not reorient rapidly in solution. For reviews of applications of solid-state NMR spectroscopy to biological systems see Torchia and VanderHart (1979), Griffin (1981), Oldfield et al. (1982), Opella (1982), Torchia (1982), Gauesh (1984), Torchia (1984) and Opella (1986). This review describes how solid-state NMR can be used to obtain structural information about proteins. Methods applicable to samples with macroscopic orientation are emphasized.

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