NMR Spectroscopy Can Characterize Proteins Encapsulated in a Sol-Gel Matrix

Wheeler, Korin E.; Nocek, Judith M.; Hoffman, Brian M.

doi:10.1021/ja066244m

Cited by 17 publications

(25 citation statements)

References 30 publications

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“…Two kinds of encapsulation are now widely used. The first is formed by nanoporous silica gels or glasses [32][33][34][35] or polyacrylamide gels [36]; the second is formed by sodium bis(2-ethylhexyl) sulfosuccinate (AOT) reverse micelles [37][38][39][40][41]. In both cases, the cage sizes can be controlled.…”

Section: Experimental Studies In the Test Tube Enhancement Of Foldingmentioning

confidence: 99%

Protein folding in confined and crowded environments

Zhou

2008

Archives of Biochemistry and Biophysics

152

137

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Confinement and crowding are two major factors that can potentially impact protein folding in cellular environments. Theories based on considerations of excluded volumes predict disparate effects on protein folding stability for confinement and crowding: confinement can stabilize proteins by over 10k B T but crowding has a very modest effect on stability. On the other hand, confinement and crowding are both predicted to favor conformations of the unfolded state which are compact, and consequently may increase the folding rate. These predictions are largely borne out by experimental studies of protein folding under confined and crowded conditions in the test tube. Protein folding in cellular environments is further complicated by interactions with surrounding surfaces and other factors. Concerted theoretical modeling and test-tube and in vivo experiments promise to elucidate the complexity of protein folding in cellular environments.The complexity of the cellular environments in which proteins function is increasingly been appreciated [1]. Potential impacts of two related, but distinct factors, confinement and macromolecular crowding, on protein folding are receiving extensive attention [2][3][4][5]. Confinement arises from encapsulation of proteins in compartments with dimensions on the scales of 10's to 100's Å, which are only moderately larger than the sizes of the proteins themselves. Examples of such compartments include the Anfinsen cage of chaperonins and the exit tunnel of ribosomes. Crowding refers to the exclusion of volumes to proteins of interest by the presence of other macromolecules. The aims of this paper are to discuss potential impacts of confinement and crowding on protein folding and to review the progress made by recent studies on protein folding in confined and crowded conditions and in cellular environments.

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Section: Experimental Studies In the Test Tube Enhancement Of Foldingmentioning

confidence: 99%

Protein folding in confined and crowded environments

Zhou

2008

Archives of Biochemistry and Biophysics

152

137

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“…The majority of cyt c resonances demonstrated small changes in line width, increasing on average by 25-35 % at 200 and 300 g L À1 PEG. Compared to the approximately twofold line-width increases for cyt c bound to cyt c peroxidase, [22] and cyt b 5 encapsulated in sol-gel, [14] this indicates that the rotational correlation time (t c ) of cyt c is weakly influenced by PEG. Resonance broadening was greater for a number of amides found in flexible loops, including Gly34, [23] which was broadened beyond detection.…”

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confidence: 93%

“…[1][2][3] Such sample conditions are accessible by NMR spectroscopy, and the effects of macromolecular crowding on protein structure and dynamics have been investigated. [4][5][6][7][8][9][10][11] Related NMR studies of macromolecular confinement have been performed by using polyacrylamide gels, [12] reverse micelles, [13] sol-gels [14] and agarose gels. [15] Generally, crowding/confinement tends to accelerate protein folding, promotes self-association and stabilises protein structure.…”

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confidence: 99%

NMR Spectroscopy Reveals Cytochrome c–Poly(ethylene glycol) Interactions

2008

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“…Sanjay et al [235,236] evidence by solid state 27 Al NMR that the adsorption of a-amylase on K-10 montmorillonite affects the Al tetrahedral sites while covalent binding occurs exclusively on the octahedral sites. More recently an NMR study [237] demonstrated for the first time that it is possible to obtain high resolution for proteins (Cyt-c, Cyt-b 5 ) entrapped in a sol-gel matrix, showing that the embedded proteins show little conformational change.…”

Section: Enzyme-host Structure Interactionsmentioning

confidence: 99%

Enzyme‐Based Bioinorganic Materials

Forano

Prévot

2007

Bio‐inorganic Hybrid Nanomaterials

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Trends in research materials currently focus on innovation in the field of intelligent or smart materials [1]. Smart materials are materials that display functionalities able to detect a change in the near environment, answer to a stimulus, modify a property, store, transfer or convert a signal, in a sense behave like living cells. The design of smart materials focuses on the concept of biomimetic materials [2][3][4] in order to reproduce specific and selective properties not deliverable by standard chemical or physical processes. Hence, there has been much effort concentrated on the development of enzyme-based biohybrid materials. Enzyme-based biohybrid materials are under much investigation for the operation of physical or chemical functions. Enzymes display active and selective properties such as molecular recognition, complexation or carrier functions, and a wide range of catalytic reactions (hydrolysis, condensation, redox reaction, isomerization, reaction transfer). Enzymes are thus very attractive as an alternative to traditional catalysts when chemical routes are difficult to apply. Enzymes are able to catalyze regio-and stereo-selective reactions with rate accelerations up to 10-17 fold [17]. They are interesting materials for realization of sensing devices, recognition systems and nanoreactors with many potential industrial developments in biocatalysis [4] for the food industry or effluent treatment [5,6], in biomedical domains for medical implants or enzyme delivery [7], in bioanalysis and affinity chromatography [8,9], and in biosensor technology [10][11][12].Engineering the development of biohybrid enzyme-based materials requires solution of the limitations of the use of enzymes due to their intrinsic fragility against the various environmental stresses and their narrow range of working conditions (e.g. short pH and temperature range). Embedding enzymes in protective matrices in order to solve these problems has been envisaged for many years [13,14]. Immobilization of enzymes in solid supports is seen as a strategy to preserve the active site, to improve the performance of the enzyme, that is, its activity, reaction rate and long-term stability, and to allow enzyme reuse. Physical and chemical properties of the solid supports such as particle size, surface area, pore diameter, mechanical j443 Bio-inorganic Hybrid Nanomaterials. Edited

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NMR Spectroscopy Can Characterize Proteins Encapsulated in a Sol-Gel Matrix

Cited by 17 publications

References 30 publications

Protein folding in confined and crowded environments

Protein folding in confined and crowded environments

NMR Spectroscopy Reveals Cytochrome c–Poly(ethylene glycol) Interactions

Enzyme‐Based Bioinorganic Materials

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