scholarly journals Front Cover: Symmetry-Directed Self-Assembly of a Tetrahedral Protein Cage Mediated by de Novo-Designed Coiled Coils (ChemBioChem 19/2017)

ChemBioChem ◽  
2017 ◽  
Vol 18 (19) ◽  
pp. 1871-1871 ◽  
Author(s):  
Somayesadat Badieyan ◽  
Aaron Sciore ◽  
Joseph D. Eschweiler ◽  
Philipp Koldewey ◽  
Ajitha S. Cristie-David ◽  
...  
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Coiled Coils ◽  
Front Cover ◽  
Protein Cage

scholarly journals Symmetry-Directed Self-Assembly of a Tetrahedral Protein Cage Mediated by de Novo-Designed Coiled Coils

ChemBioChem ◽  
2017 ◽  
Vol 18 (19) ◽  
pp. 1888-1892 ◽  
Author(s):  
Somayesadat Badieyan ◽  
Aaron Sciore ◽  
Joseph D. Eschweiler ◽  
Philipp Koldewey ◽  
Ajitha S. Cristie-David ◽  
...  
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Coiled Coils ◽  
Protein Cage

scholarly journals Front Cover: Template‐Free Self‐Assembly of Artificial De Novo Viral Coat Proteins into Nanorods: Effects of Sequence, Concentration, and Temperature (Chem. Eur. J. 47/2019)

2019 ◽  
Vol 25 (47) ◽  
pp. 10971-10971
Author(s):  
Ernesto Cazares Vargas ◽  
Martien A. Cohen Stuart ◽  
Renko de Vries ◽  
Armando Hernandez‐Garcia
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Coat Proteins ◽  
Front Cover ◽  
Viral Coat ◽  
Template Free ◽  
Viral Coat Proteins

Metal Ion Assisted Folding and Supramolecular Organization of a De Novo Designed Metalloprotein

2004 ◽  
Vol 57 (1) ◽  
pp. 33 ◽  
Author(s):  
Guido W. M. Vandermeulen ◽  
Christos Tziatzios ◽  
Dieter Schubert ◽  
Philip R. Andres ◽  
Alexander Alexeev ◽  
...  
Keyword(s):  
Protein Folding ◽  
Self Assembly ◽  
Metal Ion ◽  
De Novo ◽  
Coiled Coil ◽  
Coiled Coils ◽  
The Self ◽  
Supramolecular Organization ◽  
Low Concentrations ◽  
The Moment

This paper describes the supramolecular organization of a novel de novo designed metalloprotein, which consists of two N-terminal terpyridine modified coiled-coil protein folding motif sequences held together by an iron(II) ion. The self-assembly of the metalloprotein is the result of the interplay of metal ion complexation and protein folding, and can be manipulated by changes in concentration, temperature, and solvent. At low concentrations, folding and organization of the metalloprotein resembles that of the native coiled-coil peptide. Besides unimeric species, also dimeric and tetrameric metalloprotein assemblies were found. Several indications suggest that at least part of these unimeric species may exist as intramolecularly folded coiled-coils, however, unambiguous proof is lacking at the moment. At higher concentrations, folding and organization is dominated by the large octahedral [FeII(terpy)2] complexes (terpy = 2,2′:6′,2″-terpyridine) and considerable amounts of large, ill-defined aggregates are formed.

scholarly journals Front Cover: De Novo Design of Selective Quadruplex–Duplex Junction Ligands and Structural Characterisation of Their Binding Mode: Targeting the G4 Hot‐Spot (Chem. Eur. J. 20/2021)

2021 ◽  
Vol 27 (20) ◽  
pp. 6101-6101
Author(s):  
Laura Díaz‐Casado ◽  
Israel Serrano‐Chacón ◽  
Laura Montalvillo‐Jiménez ◽  
Francisco Corzana ◽  
Agatha Bastida ◽  
...  
Keyword(s):  
De Novo ◽  
Hot Spot ◽  
Binding Mode ◽  
De Novo Design ◽  
Front Cover ◽  
Structural Characterisation

Inside Front Cover: Self-Assembly of Diblock-Copolymer Micelles for Template-Based Preparation of PbTiO3 Nanograins (Adv. Funct. Mater. 18/2006)

2006 ◽  
Vol 16 (18) ◽  
pp. NA-NA
Author(s):  
S. Kronholz ◽  
S. Rathgeber ◽  
S. Karthäuser ◽  
H. Kohlstedt ◽  
S. Clemens ◽  
...  
Keyword(s):  
Diblock Copolymer ◽  
Self Assembly ◽  
Front Cover ◽  
Copolymer Micelles

scholarly journals Methionine-stabilized nonclassical growth within self-assembled de novo gold nanoparticles in conjunction with secondary nucleation inhibition

2021 ◽  
Author(s):  
Jitendra Sahu ◽  
Shahbaz Lone ◽  
Kalyan Sadhu
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Noble Metal Nanoparticles ◽  
Secondary Nucleation ◽  
Unique Case ◽  
Primary Particles ◽  
Growth Reaction ◽  
Aurophilic Interaction ◽  
Key Steps

Abstract The key steps for seed mediated growth of noble metal nanoparticles involve primary and secondary nucleation, which depends upon the energy barrier and ligand supersaturation standards of the medium. Herein we report the unique case of methionine (Met) controlled growth reaction, which rather proceeds via impeding secondary nucleation in presence of citrate stabilized gold nanoparticle (AuNP). The interaction between freshly generated Au+ and thioether group of Met in the medium restricts the secondary nucleation process involving further Au+ reduction. This incomplete conversion of Au+ results in a significant enhancement of the zeta (ζ) potential even at low concentration of Met. Furthermore, the aurophilic interaction of Au+ controls the self-assembly process of the in situ generated emissive nucleated particles. Nucleation of primary particles on seed surface, their segregation and time dependent conversion to larger particles within self-assembly confirm the nonclassical growth, which has further been explored with Met containing bio-inspired peptides.

scholarly journals De novo centriole formation in human cells is error-prone and does not require SAS-6 self-assembly

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Won-Jing Wang ◽  
Devrim Acehan ◽  
Chien-Han Kao ◽  
Wann-Neng Jane ◽  
Kunihiro Uryu ◽  
...  
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Human Cells ◽  
De Novo Synthesis ◽  
Current Paradigm

Vertebrate centrioles normally propagate through duplication, but in the absence of preexisting centrioles, de novo synthesis can occur. Consistently, centriole formation is thought to strictly rely on self-assembly, involving self-oligomerization of the centriolar protein SAS-6. Here, through reconstitution of de novo synthesis in human cells, we surprisingly found that normal looking centrioles capable of duplication and ciliation can arise in the absence of SAS-6 self-oligomerization. Moreover, whereas canonically duplicated centrioles always form correctly, de novo centrioles are prone to structural errors, even in the presence of SAS-6 self-oligomerization. These results indicate that centriole biogenesis does not strictly depend on SAS-6 self-assembly, and may require preexisting centrioles to ensure structural accuracy, fundamentally deviating from the current paradigm.

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