N-Terminal 33 Amino Acid Residues ofEscherichia coliRecA Protein Contribute to its Self-assembly

1995 ◽  
Vol 250 (4) ◽  
pp. 471-483 ◽  
Author(s):  
Tsutomu Mikawa ◽  
Ryoji Masui ◽  
Tomoko Ogawa ◽  
Hideyuki Ogawa ◽  
Seiki Kuramitsu
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Amino Acid Residues

Engineering two mutants of cDNA-encoding G2 subunit of soybean glycinin capable of self-assembly in vitro and rich in methionine

Biologia ◽  
2007 ◽  
Vol 62 (4) ◽  
Author(s):  
Reda Sammour
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Seed Quality ◽  
Amino Acid Residues ◽  
Methionine Residues

AbstractThe main goal of this work was to make the cDNA-encoding subunit G2 of soybean glycinin, capable of self-assembly in vitro and rich in methionine residues. Two mutants (pSP65/G4SacG2 and pSP65/G4SacG2HG4) were therefore constructed. The constructed mutants were successfully assembled in vitro into oligomers similar to those occurred in the seed. The successful self-assembly was due to the introduction of Sac fragment of Gy4 (the codons of the first 21 amino acid residues), which reported to be the key element in self-assembly into trimers. The mutant pSP65/G4SacG2HG4 included the acidic chain of Gy4 (HG4), which was previously molecularly modified to have three methionine residues. This mutant will be useful in the efforts to improve the seed quality.

Mimicking the Function of Eggshell Matrix Proteins: The Role of Multiplets of Charged Amino Acid Residues and Self-Assembly of Peptides in Biomineralization

2005 ◽  
Vol 44 (34) ◽  
pp. 5476-5479 ◽  
Author(s):  
Parayil Kumaran Ajikumar ◽  
Subramanian Vivekanandan ◽  
Rajamani Lakshminarayanan ◽  
Seetharama D. S. Jois ◽  
R. Manjunatha Kini ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Matrix Proteins ◽  
Amino Acid Residues ◽  
Eggshell Matrix

Amino Acid Residues Vary the Self‐Assembly and Photophysical Properties of Diphenylamine‐Cyanostilbene‐Capped Amphiphiles

ChemPhotoChem ◽  
2020 ◽  
Vol 4 (7) ◽  
pp. 481-486
Author(s):  
Mei‐Yu Yeh ◽  
Tzu‐Yu Tseng ◽  
Hui‐Chun Hsieh ◽  
Bao‐Xing Wu ◽  
Yi‐Shun Liao ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Photophysical Properties ◽  
The Self ◽  
Amino Acid Residues

Differential supramolecular organisation of Fmoc-dipeptides with hydrophilic terminal amino acid residues by biocatalytic self-assembly

Soft Matter ◽  
2012 ◽  
Vol 8 (45) ◽  
pp. 11565 ◽  
Author(s):  
Meghan Hughes ◽  
Louise S. Birchall ◽  
Karim Zuberi ◽  
Lynsey A. Aitken ◽  
Sisir Debnath ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Supramolecular Organisation ◽  
Terminal Amino

scholarly journals THE PROCESS OF SELF-ORGANIZATION IN LOW-CONCENTRATED AQUEOUS SYSTEMS BASED ON N-ACETYL-L-CYSTEINE, L-CYSTEINE AND SILVER ACETATE

2020 ◽  
pp. 70-82
Author(s):  
Дмитрий Вадимович Аверкин ◽  
Дмитрий Викторович Вишневецкий ◽  
Владимир Романович Петров ◽  
Светлана Дмитриевна Хижняк ◽  
Павел Михайлович Пахомов
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Uv Spectroscopy ◽  
Self Organization ◽  
Amino Acid Residues ◽  
Silver Acetate ◽  
The Core ◽  
Organization Process ◽  
Silver Cations ◽  
Comprehensive Study

Проведено комплексное исследование процесса самоорганизации при сливании низкоконцентрированных водных растворов N-ацетил-L-цистеина и ацетата серебра. Все стадии самоорганизации изучены c помощью измерения величины рН, методов вискозиметрии, УФ спектроскопии и динамического светорассеяния (ДСР). Установлено, что началом самосборки является замена водорода в меркаптогруппе аминокислоты на катион серебра с образованием молекулы меркаптида серебра (МС). Далее происходит образование цепочек вида (-Ag-S(NCys)-Ag-S(NCys)-), при этом происходит протонирование аминокислотных остатков N-ацетил-L-цистеина. Предложен механизм самоорганизации в водном растворе N-ацетил-L-цистеина и ацетата серебра (N-ацетилцистеин-серебряный раствор - НАЦ), заключающийся в образовании агрегатов типа «ядро-оболочка». «Ядро» агрегатов состоит из цепочек вида (-Ag-S(NCys)-Ag-S(NCys)-), «оболочка» агрегатов состоит из протонированных аминокислотных остатков. Связывание таких агрегатов происходит посредством образования связей с ацетат-анионами. A comprehensive study of the self-organization process during the draining of low-concentration aqueous solutions of N-acetyl-L-cysteine and silver acetate was carried out. All stages of self-organization have been studied using pH measurements, viscometry, UV spectroscopy, and dynamic light scattering (DLS). It was found that the first stage of self-assembly is the replacement of hydrogen in the mercapto group of an amino acid with a silver cation with the formation of a silver mercaptide (MS) molecule. Further, the formation of chains of the form (-Ag-S(NCys)-Ag-S(NCys)-) occurs, while excess electron density is retained in amino acid residues, leading to the interaction of chains with both silver cations and undissociated silver acetate molecules , with the formation of clusters. The mechanism of self-organization of the system as the formation of the aggregates of the «core-shell» type is proposed. The «core» consists of chains of the form (-Ag-S(NCys)-Ag-S(NCys)-), the «shell» consists of protonated N-acetyl-L-cysteine resides. Further bonding of aggregates into clusters occurs through free acetic acid anions.

scholarly journals Hypochlorite-induced oxidative modification of fibrinogen

2019 ◽  
Vol 484 (3) ◽  
pp. 367-371
Author(s):  
L. V. Yurina ◽  
A. D. Vasilyeva ◽  
A. E. Bugrova ◽  
M. I. Indeykina ◽  
A. S. Kononikhin ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Oxidative Damage ◽  
Self Assembly ◽  
Protein Electrophoresis ◽  
Oxidative Modification ◽  
Cross Linking ◽  
Amino Acid Residues ◽  
Fibrin Network

Oxidation of fibrinogen with hypochlorite inhibited the fibrin network self-assembly even at the lowest concentration of the oxidant. The analysis of the results of protein electrophoresis at this hypochlorite concentration showed the absence of fragmentation of the protein and covalent cross-linking of its chains. The study of the areas responsible for the conversion of fibrinogen into fibrin by mass spectrometry showed that they are not subject to oxidative damage. However, we identified oxidized amino acid residues, which could affect the protofibril aggregation.

Amino acid sequence controls the self-assembled superstructure morphology of N-acetylated tri-β3-peptides

2015 ◽  
Vol 87 (9-10) ◽  
pp. 1021-1028 ◽  
Author(s):  
Rania S. Seoudi ◽  
Annette Dowd ◽  
Mark Del Borgo ◽  
Ketav Kulkarni ◽  
Patrick Perlmutter ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Far Infrared ◽  
High Symmetry ◽  
Amino Acid Residues ◽  
Cross Sectional ◽  
Self Assembling ◽  
Afm Imaging ◽  
High Degree ◽  
Degree Of Similarity

AbstractPeptides based on unnatural β3-amino acids offer a versatile platform for the design of self-assembling nanostructures due to the folding stability of the 14-helix and the high symmetry of the side chains inherent in this geometry. We have previously described that N-terminal acetylation (Ac-) forms a supramolecular self-assembly motif that allows β3-peptides to assemble head-to-tail into a helical nanorod which then further bundles into hierarchical superstructures. Here we investigate the effect of the topography of the 14-helical nanorod on lateral self-assembly. Specifically, we report on the variations in the superstructure of three isomeric peptides comprising the same three β3-amino acid residues: β3-leucine (L), β3-isoleucine (I) β3-alanine (A) to give peptides Ac-β3[LIA], Ac-β3[IAL] and Ac-β3[ALI]. AFM imaging shows markedly different superstructures for the three peptides. Well defined synchrotron far-infrared spectra reveal uniform geometries with a high degree of similarity between the isomeric peptides in the amide modes of the 400–650 wavenumber range. Far-IR also confirms that the C-terminal carboxyl group is free in the assemblies, thus it is solvated in the dispersant. Hence, the differences in the superstructures formed by the fibers are defined primarily by van der Waals energy minimization between the varied cross sectional morphologies of the core nanorods.

Mimicking the Function of Eggshell Matrix Proteins: The Role of Multiplets of Charged Amino Acid Residues and Self-Assembly of Peptides in Biomineralization

2005 ◽  
Vol 117 (34) ◽  
pp. 5612-5615 ◽  
Author(s):  
Parayil Kumaran Ajikumar ◽  
Subramanian Vivekanandan ◽  
Rajamani Lakshminarayanan ◽  
Seetharama D. S. Jois ◽  
R. Manjunatha Kini ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Matrix Proteins ◽  
Amino Acid Residues ◽  
Eggshell Matrix

scholarly journals Self-Assembly of Supramolecular Architectures by the Effect of Amino Acid Residues of Quaternary Ammonium Pillar[5]arenes

2020 ◽  
Vol 21 (19) ◽  
pp. 7206
Author(s):  
Anastasia Nazarova ◽  
Dmitriy Shurpik ◽  
Pavel Padnya ◽  
Timur Mukhametzyanov ◽  
Peter Cragg ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
1H Nmr Spectroscopy ◽  
Water Soluble ◽  
Amino Acid Residues ◽  
Acid Moiety ◽  
Supramolecular Architectures ◽  
First Case ◽  
Amino Acid Moiety ◽  
Methyl Orange Dye

Novel water-soluble multifunctional pillar[5]arenes containing amide-ammonium-amino acid moiety were synthesized. The compounds demonstrated a superior ability to bind (1S)-(+)-10-camphorsulfonic acid (S-CSA) and methyl orange dye depending on the nature of the substituent, resulting in the formation one-to-one complexes with both guests. The formation of host-guest complexes was confirmed by ultraviolet (UV), circular dichroism (CD) and 1H NMR spectroscopy. This work demonstrates the first case of using S-CSA as a chiral template for the non-covalent self-assembly of architectures based on pillar[5]arenes. It was shown that pillar[5]arenes with glycine or L-alanine fragments formed aggregates with average hydrodynamic diameters (d) of 165 and 238 nm, respectively. It was established that the addition of S-CSA to the L-alanine-containing derivative led to the formation of micron-sized aggregates with d of 713 nm. This study may advance the design novel stereoselective catalysts and transmembrane amino acid channels.

Sign in / Sign up

Export Citation Format

Share Document