scholarly journals Artificial Protein Hydrogel Materials

1998 ◽  
Vol 550 ◽  
Author(s):  
W. A. Petka ◽  
J. L. Harden ◽  
J. K. Sakata ◽  
D. A. Tirrell
Keyword(s):  
Viscoelastic Properties ◽  
Triblock Copolymer ◽  
Leucine Zipper ◽  
Recombinant Dna ◽  
Coiled Coil ◽  
Water Soluble ◽  
Artificial Proteins ◽  
New Class ◽  
Artificial Protein ◽  
Behavior Characteristic

AbstractRecombinant DNA methods were used to create a new class of artificial proteins that undergo reversible gelation in response to changes in pH or temperature. These proteins consist of terminal a-helical “leucine zipper” domains flanking a central, water-soluble polvelectrolyte segment. The formation of coiled-coil aggregates of the terminal domains in near-neutral pH solution triggers formation of a polymer hydrogel, with the central polyelectrolyte segment retaining solvent and preventing precipitation of the chains. Dissociation of the coiled-coil aggregates through elevation of pH or temperature causes dissolution of the gel and a return to the viscous behavior characteristic of a polymer solution. The pH and temperature range of the hydrogel state and its viscoelastic properties may be systematically varied through precise changes of the length, composition and charge density of the terminal and central blocks. Such control is of value in designing hydrogels with predetermined physical properties and makes these biosynthetic triblock copolymer systems attractive candidates for use in molecular and cellular encapsulation and in controlled reagent delivery.

Size Control of Block Polymer Templated Mesoporous Silicate Materials

2000 ◽  
Vol 628 ◽  
Author(s):  
Takeo Yamada ◽  
Keisuke Asai ◽  
Kenkichi Ishigure ◽  
Akira Endo ◽  
Hao S. Zhou ◽  
...  
Keyword(s):  
Mesoporous Materials ◽  
Molecular Sieve ◽  
Mesoporous Material ◽  
Triblock Copolymer ◽  
Size Control ◽  
Block Polymer ◽  
New Class ◽  
Mesoporous Silicate ◽  
Cubic Structure ◽  
Silicate Materials

ABSTRACTMesoporous materials have attracted considerable interest because of applications in molecular sieve, catalyst, and adsorbent. It will be useful for new functional device if functional molecules can be incorporated into the pore of mesoporous material. However, it is necessary to synthesize new mesoporous materials with controlled large pore size. Recently, new class of mesoporous materials has been prepared using triblock copolymer as a template. In this paper, we reported that hexagonal and cubic structure silicate mesoporous materials can be synthesized through triblock copolymer templating, and their size was controlled by synthesis condition at condensation.

Sticky ends in a self-assembling ABA triblock copolymer: the role of ureas in stimuli-responsive hydrogels

2019 ◽  
Vol 4 (1) ◽  
pp. 91-102 ◽  
Author(s):  
Ryan T. Shafranek ◽  
Joel D. Leger ◽  
Song Zhang ◽  
Munira Khalil ◽  
Xiaodan Gu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Viscoelastic Properties ◽  
Triblock Copolymer ◽  
Thermal Response ◽  
Stimuli Responsive ◽  
Self Assembling ◽  
Polymeric Hydrogels ◽  
Aba Triblock Copolymer ◽  
Responsive Hydrogels

Directed self-assembly in polymeric hydrogels allows tunability of thermal response and viscoelastic properties.

Leucine Is the Most Stabilizing Aliphatic Amino Acid in thedPosition of a Dimeric Leucine Zipper Coiled Coil

Biochemistry ◽  
1997 ◽  
Vol 36 (41) ◽  
pp. 12567-12573 ◽  
Author(s):  
Jaideep Moitra ◽  
Lászlo Szilák ◽  
Dmitry Krylov ◽  
Charles Vinson
Keyword(s):  
Amino Acid ◽  
Leucine Zipper ◽  
Coiled Coil ◽  
Aliphatic Amino Acid

New Approach to Detect Coiled Coil and Leucine Zipper Motifs in Protein Sequences

2018 ◽  
Vol 25 (11) ◽  
pp. 1278-1283
Author(s):  
Dinko Osmankovic ◽  
Semir Doric ◽  
Naris Pojskic ◽  
Lada Lukic Bilela
Keyword(s):  
Leucine Zipper ◽  
Coiled Coil ◽  
Protein Sequences ◽  
New Approach

Polymer Coiled-Coil Conjugates: Potential for Development as a New Class of Therapeutic “Molecular Switch”

2011 ◽  
Vol 12 (1) ◽  
pp. 19-27 ◽  
Author(s):  
Samuel P. E. Deacon ◽  
Bojana Apostolovic ◽  
Rodrigo J. Carbajo ◽  
Anne-Kathrin Schott ◽  
Konrad Beck ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Molecular Switch ◽  
New Class

scholarly journals Spectral Tuning of Chlorophylls in Proteins – Electrostatics vs. Ring Deformation

2020 ◽  
Author(s):  
Yigal Lahav ◽  
Dror Noy ◽  
Igor Schapiro
Keyword(s):  
Absorption Spectra ◽  
Conformational Dynamics ◽  
Spectral Shift ◽  
Water Soluble ◽  
Conformational Sampling ◽  
Protein Electrostatics ◽  
Spectral Tuning ◽  
Photosynthetic Complexes ◽  
Artificial Protein ◽  
Ring Deformation

In photosynthetic complexes, tuning of chlorophyll light-absorption spectra by the protein environment is crucial to their efficiency and robustness. Water Soluble Chlorophyll-binding Proteins from <i>Brassicaceae</i> (WSCPs) are useful for studying spectral tuning mechanisms due to their symmetric homotetramer structure, the ability to rigorously modify the chlorophyll’s protein surroundings, and the availability of crystal structures. Here, we present a rigorous analysis based on hybrid Quantum Mechanics and Molecular Mechanics simulations with conformational sampling to quantify the relative contributions of steric and electrostatic factors to the absorption spectra of WSCP-chlorophyll complexes. We show that when considering conformational dynamics, chlorophyll ring deformation accounts for about one-third of the spectral shift, whereas protein electrostatics accounts for the remaining two-thirds. From a practical perspective, protein electrostatics is easier to manipulate than chlorophyll conformations, thus, it may be more readily implemented in designing artificial protein-chlorophyll complexes with desired spectral shift.

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