Photoinduced conformational transition of polypeptide membrane composed of poly(L-glutamic acid) containing pararosaniline groups in the side chains

1988 ◽  
Vol 21 (12) ◽  
pp. 3419-3424 ◽  
Author(s):  
Morimasa Sato ◽  
Takatoshi Kinoshita ◽  
Akira Takizawa ◽  
Yoshiharu Tsujita
Keyword(s):  
Glutamic Acid ◽  
Conformational Transition ◽  
Side Chains

scholarly journals Effects of Amino Acid Side-Chain Length and Chemical Structure on Anionic Polyglutamic and Polyaspartic Acid Cellulose-Based Polyelectrolyte Brushes

Polymers ◽  
2021 ◽  
Vol 13 (11) ◽  
pp. 1789
Author(s):  
Dmitry Tolmachev ◽  
George Mamistvalov ◽  
Natalia Lukasheva ◽  
Sergey Larin ◽  
Mikko Karttunen
Keyword(s):  
Glutamic Acid ◽  
Chain Length ◽  
Chemical Structure ◽  
Side Chain ◽  
Side Chains ◽  
Side Chain Length ◽  
Polyelectrolyte Brushes ◽  
Grafting Density ◽  
The Difference ◽  
Cellulose Surface

We used atomistic molecular dynamics (MD) simulations to study polyelectrolyte brushes based on anionic α,L-glutamic acid and α,L-aspartic acid grafted on cellulose in the presence of divalent CaCl2 salt at different concentrations. The motivation is to search for ways to control properties such as sorption capacity and the structural response of the brush to multivalent salts. For this detailed understanding of the role of side-chain length, the chemical structure and their interplay are required. It was found that in the case of glutamic acid oligomers, the longer side chains facilitate attractive interactions with the cellulose surface, which forces the grafted chains to lie down on the surface. The additional methylene group in the side chain enables side-chain rotation, enhancing this effect. On the other hand, the shorter and more restricted side chains of aspartic acid oligomers prevent attractive interactions to a large degree and push the grafted chains away from the surface. The difference in side-chain length also leads to differences in other properties of the brush in divalent salt solutions. At a low grafting density, the longer side chains of glutamic acid allow the adsorbed cations to be spatially distributed inside the brush resulting in a charge inversion. With an increase in grafting density, the difference in the total charge of the aspartic and glutamine brushes disappears, but new structural features appear. The longer sides allow for ion bridging between the grafted chains and the cellulose surface without a significant change in main-chain conformation. This leads to the brush structure being less sensitive to changes in salt concentration.

scholarly journals Effects of Amino Acid Side Chain Length and Chemical Structure on Anionic Polyglutamic and Polyaspartic Acid Cellulose-Based Polyelectrolyte Brushes

2021 ◽  
Author(s):  
Dmitry Tolmachev ◽  
George Mamistvalov ◽  
Natalia Lukasheva ◽  
Sergey Larin ◽  
Mikko Karttunen
Keyword(s):  
Glutamic Acid ◽  
Chain Length ◽  
Chemical Structure ◽  
Side Chain ◽  
Side Chains ◽  
Side Chain Length ◽  
Polyelectrolyte Brushes ◽  
Grafting Density ◽  
The Difference ◽  
Cellulose Surface

We used atomistic molecular dynamics (MD) simulations to study polyelectrolyte brushes based on anionic α-L-glutamic acid and α-L-aspartic acid grafted on cellulose in the presence of divalent CaCl2 salt at different concentrations. The motivation is the search of the ways to control properties such as sorption capacity and the structural response of the brush to multivalent salts. For this detailed understanding of the role of side chain length, chemical structure and their interplay is required. It was found that in the case of glutamic acid oligomers, the longer side chains facilitate attractive interactions with the cellulose surface, which forces the grafted chains to lie down on the surface. The additional methylene group in the side chain enables side chain rotation enhancing this effect. On the other hand, the shorter and more restricted side chains of aspartic acid oligomers prevent attractive interactions to a large degree and push the grafted chains away from the surface. The difference in side chain length also leads to differences in other properties of the brush in divalent salt solutions. At a low grafting density, the longer side chains of glutamic acid allow the adsorbed cations to be spatially distributed inside the brush resulting in a charge inversion. With an increase in grafting density, the difference in the total charge of the aspartic and glutamine brushes disappears, but new structural features appear. The longer sides allow for ion bridging between the grafted chains and the cellulose surface without a significant change in main chain conformation. This leads to the brush structure being less sensitive to changes in salt concentration.

Reversible conformational changes induced by light in poly(L-glutamic acid) with photochromic side chains

1980 ◽  
Vol 102 (18) ◽  
pp. 5913-5915 ◽  
Author(s):  
Osvaldo Pieroni ◽  
Julien L. Houben ◽  
Adriano Fissi ◽  
Paolo Costantino ◽  
Francesco Ciardelli
Keyword(s):  
Glutamic Acid ◽  
Conformational Changes ◽  
Side Chains

scholarly journals Glutamic acid 327 in the sheep α 1 isoform of Na+,K+-ATPase is a pivotal residue for cation-induced conformational changes

1995 ◽  
Vol 309 (1) ◽  
pp. 187-194 ◽  
Author(s):  
C L Johnson ◽  
T A Kuntzweiler ◽  
J B Lingrel ◽  
C G Johnson ◽  
E T Wallick
Keyword(s):  
Glutamic Acid ◽  
Conformational Changes ◽  
Conformational Transition ◽  
Cation Binding ◽  
Monovalent Cations ◽  
Wild Type ◽  
Binding Studies ◽  
Ouabain Binding ◽  
Na Ions ◽  
Inhibition Curve

The cation binding characteristics of the mutant E327A formed in the sheep alpha 1 isoform of the Na+,K(+)-ATPase were examined using [3H]ouabain binding as a function of monovalent cation concentrations. Equilibrium competition binding assays in the presence of Mg2+, inorganic phosphate and various amounts of unlabelled ouabain indicated that both wild-type sheep alpha 1 protein and the E327A mutant expressed in 3T3 cells had similar affinities for ouabain (KD = 1.53 and 1.31 nM respectively). Sodium inhibition of ouabain binding appeared competitive in both enzymes. However, binding of three Na+ ions was required to explain the steep character of the Na+ inhibition curve for the wild-type Na+,K(+)-ATPase (Ki = 12.8 +/- 1.6 mM), whereas the binding of two Na+ ions was detected for the mutant E327A (Ki = 19.2 +/- 2.5 mM). Potassium binding of [3H]ouabain binding displayed a partially competitive nature with Hill coefficients of 2 for both wild-type sheep alpha 1 (Ki = 0.743 +/- 0.044 mM) and E327A (Ki = 0.875 +/- 0.067 mM). At concentrations of K+ above 10 mM, the sheep alpha 1 competition curve levelled off whereas the inhibition curve for E327A displayed a stimulation in ouabain binding. This stimulation in [3H]ouabain binding also occurred with Rb+, Cs+ and Li+, but was never observed with choline or Na+, suggesting that this effect was not due to ionic strength. From these [3H]ouabain-binding studies, it is obvious that the mutant enzyme E327A in the presence of Mg2+, Pi and ouabain, interacts with monovalent cations in a unique fashion. One interpretation of these data is that the glutamic acid residue at position 327 is involved in a conformational transition induced by the binding of monovalent cations to the Na+,K+-ATPase and that this transition is inhibited by the mutation of E327A.

Sodium versus potassium effects on the glutamic acid side-chains interaction on a heptapeptide

2014 ◽  
Vol 13 (03) ◽  
pp. 1440004 ◽  
Author(s):  
Eliana K. Asciutto ◽  
Timothy Gaborek ◽  
Jeffry D. Madura
Keyword(s):  
Glutamic Acid ◽  
Pure Water ◽  
Three Dimensional ◽  
Side Chains ◽  
Saline Environment ◽  
Polyproline Ii ◽  
Peptide Conformations ◽  
Free Energy Landscapes ◽  
The Stability ◽  
Α Helix

Equilibrium peptide conformations in solution, especially in the presence of salts, has been of interest for several decades. The fundamental interactions that determine the dominant peptide conformations in solution have been experimentally and computationally probed; however, a unified understanding has not yet emerged. In a previous study, we performed metadynamics simulations on the heptapeptide AEAAAEA in Sodium Chloride ( NaCl ) and Potassium Chloride ( KCl ) solutions at concentrations ranging from 0.5–2.0 M. Using a three-dimensional collective variable coordinate system, we computed the free energy landscapes in each saline environment as well as in pure water. We found that the presence of Na + and K + ions induces some changes in the stability of the conformers that define the state space, but does not alter the overall energetics between conformers and does not favor helical conformations. We investigate here, how the presence of salts ( NaCl and KCl ) affects the glutamic–glutamic interaction and its consequences on the stability of each equilibrium conformation. We perform this study through fixed backbone simulations for the most populated conformations identified in our previous work: the α-helix, 310-helix, π-helix, the extended polyproline II (PPII) and 2.51-helix conformations. It was found that for each conformation, there exists stable substates determined by the glutamic acid side-chains distance and orientation, and that Na + and K + cations (de)stabilize preferentially each conformation. It was also found that intramolecular single water mediated hydrogen bonds play a crucial role in the observed (de) stabilization of each equilibrium conformation.

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