Influence of Proline on the Thermostability of the Active Site and Membrane Arrangement of Transmembrane Proteins

Perálvarez-Marín, Àlex; Lórenz-Fonfrı́a, Vı́ctor A.; Simón‐Vázquez, Rosana; Gomariz, María; Meseguer, Inmaculada; Querol, Enric; Padrós, Esteve

doi:10.1529/biophysj.108.136747

Cited by 30 publications

(25 citation statements)

References 64 publications

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“…The decreasing in the Cdl value is normally attributed to the replacement of the adsorbed water molecules at the metal surface by Met molecules that have a lower dielectric constant [43] . Thus, it can be concluded that the Met molecule have adsorbed on steel surface, then formed a homogeneous film, and the adsorption number perfect due to the molecular shape of Pro molecule is smaller and the molecular rigidity is stronger than Met molecule [44][45][46] . When the concentration of Pro is high, the quality of Met/Pro inhibition films is poor due to the competitive adsorption between Met and Pro molecules on iron surface.…”

Section: Molecular Dynamic Simulationsmentioning

confidence: 98%

“…The DCl-of Met system is larger than that of Pro system, which indicates that the migration speed of Cl -ion Met inhibition films is slower than that in Pro inhibition films. This may be because the molecular shape of Pro molecule is smaller and the molecular rigidity is stronger than Met molecule, thus, the compactness or quality of Pro inhibition films is higher than that of Met inhibition films [44][45][46] . Even though, this molecular structure advantages are not reflected on the single Met and Pro inhibitors due to the adsorption capability of Met molecule is stronger than that of Pro molecule on iron surface, the inhibition effect of Met/Pro compound inhibitor can be enhanced by Met molecule combining with Pro molecule due to this molecular structure advantages.…”

Section: Dynamic Simulationmentioning

confidence: 99%

“…Thus, while the concentration of Pro is low, the Met and Pro molecules can adsorb on iron surface and 11 form a dense film with a major component of Met molecule and a minor component of the Pro molecule. Pro molecule can fill in the leak of Met inhibition films and make the films perfect due to the molecular shape of Pro molecule is smaller and the molecular rigidity is stronger than Met molecule [44][45][46] . When the concentration of Pro is high, the quality of Met/Pro inhibition films is poor due to the competitive adsorption between Met and Pro molecules on iron surface.…”

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Inhibition of carbon steel corrosion in phase-change-materials solution by methionine and proline

et al. 2016

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Section: Molecular Dynamic Simulationsmentioning

confidence: 98%

Section: Dynamic Simulationmentioning

confidence: 99%

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Inhibition of carbon steel corrosion in phase-change-materials solution by methionine and proline

et al. 2016

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“…It is generally assumed that the absorbance maximum of the WT is defined by the protonation of the Schiff base (SB) and the interactions of retinal with the binding pocket. Therefore it reflects the conformation of retinal and the protein domain in the vicinity of the retinal moiety . When exposed to elevated temperatures, membrane proteins lose their functionality and denature.…”

Section: Resultsmentioning

confidence: 99%

“…When exposed to elevated temperatures, membrane proteins lose their functionality and denature. In the case of bR, the conformation of the active site is affected as well . To examine the effect of the substitution of the three Glu for Gln (Fig.…”

Section: Resultsmentioning

confidence: 99%

The effect of triple glutamic mutations E9Q/E194Q/E204Q on the structural stability of bacteriorhodopsin

et al. 2014

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In the present study, we report on the structural features of the bacteriorhodopsin triple mutant E9Q/E194Q/E204Q (3Glu) of bacteriorhodopsin by combining experimental and molecular dynamics (MD) approaches. In 3Glu mutant, Glu9, Glu194 and Glu204 residues located at the extracellular side of the protein were mutated altogether to glutamines. UV-visible and differential scanning calorimetry experiments served as diagnostic tools for monitoring the resistance against thermal stress of the active site and the tertiary structures of the 3Glu. The analyses of the UV-visible thermal difference spectra demonstrate that the spectral forms at room temperature and the thermal unfolding path differ in the wild-type bacteriorhodopsin and the 3Glu. Even with these spectral differences, the thermal unfolding of the active site occurs at rather similar melting temperatures in both proteins. A noteworthy consequence of the mutations is the altered two-dimensional packing revealed by the lack of the pre-transition peak in differential scanning calorimetry traces of 3Glu mutant, as previously detected in wild-type and the corresponding single mutants. The infrared spectroscopy data agree with the loss of paracrystalinity, illustrating a substantial conversion of a II to a I helical conformation in the 3Glu mutant. Molecular dynamics simulations show higher dynamics flexibility of most of the extracellular regions of 3Glu, which may account for the somewhat lower tertiary structural stability of the mutated protein. Finally, hydrogen bond analysis reveals that the mutated Glu194 and Glu204 residues create~50% less hydrogen bonds with water molecules compared to wild-type bacteriorhodopsin. These results exemplify the role of the water hydrogen-bonding network for structural integrity and conformational flexibility of bacteriorhodopsin.Abbreviations 3Glu, bacteriorhodopsin triple mutant E9Q/E194Q/E204Q; 3GluO, 3Glu opsin; bO, bacterioopsin; bR, bacteriorhodopsin; bRRT, ground state (RT) spectral form; DSC, differential scanning calorimetry; EC, extracellular; MD, molecular dynamics; PDB, Protein Data Bank; rmsf, root mean square fluctuations; SB, Schiff base; TDS, thermal difference spectra; WT, wild-type bacteriorhodopsin.

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Mutation in BAG3 causes severe dominant childhood muscular dystrophy

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Muntoni

Burton

et al. 2009

Annals of Neurology

335

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Objective-Myofibrillar myopathies (MFM) are morphologically distinct but genetically heterogeneous muscular dystrophies in which disintegration of Z disks and then of myofibrils is followed by ectopic accumulation of multiple proteins. Cardiomyopathy, neuropathy, and dominant inheritance are frequent associated features. Mutations in αB-crystallin, desmin, myotilin, Zasp, or filamin-C can cause MFM, and were detected in 32/85 patients of the Mayo MFM cohort. Bag3, another Z-disk associated protein, has antiapoptotic properties and its targeted deletion in mice causes fulminant myopathy with early lethality. We therefore searched for mutations in BAG3 in 53 unrelated MFM patients.Methods-We searched for mutations in BAG3 by direct sequencing and excluded polymorphism using allele-specific PCR in relatives and 200 control subjects. We analyzed structural changes in muscle by histochemistry, immunocytochemistry and electron microscopy, examined mobility of the mutant Bag3 by nondenaturing electrophoresis, and searched for abnormal aggregation of the mutant protein in COS-7 cells.Results-We identified a heterozygous p.Pro209Leu mutation in three patients. All presented in childhood, had progressive limb and axial muscle weakness, and developed cardiomyopathy and severe respiratory insufficiency in their teens; two had rigid spines and one a peripheral neuropathy. Electron microscopy showed disintegration of Z disks, extensive accumulation of granular debris and larger inclusions, and apoptosis of 8% of the nuclei. On nondenaturing electrophoresis of muscle extracts, the Bag3 complex migrated faster in patient than control extracts, and expression of FLAG-labeled mutant and wild-type Bag3 in COS cells revealed abnormal aggregation of the mutant protein.Interpretation-We conclude mutation in Bag3 defines a novel severe autosomal dominant childhood muscular dystrophy.Myofibrillar myopathies (MFMs) represent a morphologically distinct but genetically heterogeneous subset of muscular dystrophies. Cardiomyopathy, peripheral neuropathy, and dominant inheritance are frequent associated features.1 -7 The histologic findings are similar in that disintegration of the myofiber Z disk is an early pathologic alteration; this is followed

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Influence of Proline on the Thermostability of the Active Site and Membrane Arrangement of Transmembrane Proteins

Cited by 30 publications

References 64 publications

Inhibition of carbon steel corrosion in phase-change-materials solution by methionine and proline

Inhibition of carbon steel corrosion in phase-change-materials solution by methionine and proline

The effect of triple glutamic mutations E9Q/E194Q/E204Q on the structural stability of bacteriorhodopsin

Mutation in BAG3 causes severe dominant childhood muscular dystrophy

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