Bis(β-diketonate) ligands for the synthesis of bimetallic complexes of TiIII, VIII, MnIII and FeIII with a triple-helix structure

1997 ◽  
pp. 1561-1562 ◽  
Author(s):  
Vincent A. Grillo ◽  
Elisa J. Seddon ◽  
Craig M. Grant ◽  
Guillem Aromí ◽  
John C. Bollinger ◽  
...  
Keyword(s):  
Triple Helix ◽  
Bimetallic Complexes ◽  
Helix Structure

scholarly journals A neutral polysaccharide with a triple helix structure from ginger: Characterization and immunomodulatory activity

2021 ◽  
Vol 350 ◽  
pp. 129261
Author(s):  
Xiaolong Yang ◽  
Siqing Wei ◽  
Xiaoming Lu ◽  
Xuguang Qiao ◽  
Jesus Simal-Gandara ◽  
...  
Keyword(s):  
Triple Helix ◽  
Immunomodulatory Activity ◽  
Helix Structure

Triple Helix, Quadruple Helix and Quintuple Helix and How Do Knowledge, Innovation and the Environment Relate To Each Other?

2012 ◽  
pp. 535-565
Author(s):  
Elias Carayannis ◽  
David F.J. Campbell
Keyword(s):  
Sustainable Development ◽  
Triple Helix ◽  
Social Ecology ◽  
Quadruple Helix ◽  
Natural Environments ◽  
Structure Model ◽  
Triple Helix Model ◽  
Knowledge Innovation ◽  
Quintuple Helix ◽  
Helix Structure

This article develops an inter-disciplinary and trans-disciplinary framework of analysis that relates knowledge, innovation and the environment (natural environments) to each other. For that purpose the five-helix structure model of the Quintuple Helix is being introduced. The Triple Helix model, designed by Etzkowitz and Leydesdorff (2000), focuses on the relations of universities, industry and governments. The Quadruple Helix (Carayannis & Campbell, 2009) blends in the perspective of a media-based and culture-based public. The Quintuple Helix finally frames knowledge and innovation in the context of the environment (natural environments). Therefore, the Quintuple Helix can be interpreted as an approach in line with sustainable development and social ecology. “Eco-innovation” and “eco-entrepreneurship” should be processed in such a broader understanding of knowledge and innovation.

Determination of G*G.cntdot.C triple-helix structure by molecular modeling and vibrational spectroscopy

1993 ◽  
Vol 115 (10) ◽  
pp. 4264-4270 ◽  
Author(s):  
Mohammed Ouali ◽  
Richard Letellier ◽  
Jian Sheng Sun ◽  
Alain Akhebat ◽  
Frederic Adnet ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Vibrational Spectroscopy ◽  
Triple Helix ◽  
Helix Structure

The collagen triple-helix structure

1997 ◽  
Vol 15 (8-9) ◽  
pp. 545-554 ◽  
Author(s):  
Barbara Brodsky ◽  
John A.M. Ramshaw
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Structure

Molecular Dynamics Investigations on the Effect ofdAmino Acid Substitution in a Triple-Helix Structure and the Stability of Collagen

2009 ◽  
Vol 113 (26) ◽  
pp. 8983-8992 ◽  
Author(s):  
V. Punitha ◽  
S. Sundar Raman ◽  
R. Parthasarathi ◽  
V. Subramanian ◽  
J. Raghava Rao ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Triple Helix ◽  
Helix Structure ◽  
The Stability

scholarly journals Polypurine/polypyrimidine hairpins form a triple helix structure at low pH

1990 ◽  
Vol 18 (22) ◽  
pp. 6523-6529 ◽  
Author(s):  
Margret M.W. Mooren ◽  
David E. Pulleyblank ◽  
Sybren S. Wijmenga ◽  
Marcel J.J. Blommers ◽  
Cornelis W. Hilbers
Keyword(s):  
Triple Helix ◽  
Low Ph ◽  
Helix Structure

scholarly journals Anionic surfactant sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen by ultrasensitive microcalorimetry

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Jie Zhang ◽  
Chunhua Wang ◽  
Fengteng Zhang ◽  
Wei Lin
Keyword(s):  
Thermal Stability ◽  
Conformational Changes ◽  
Triple Helix ◽  
Striking Difference ◽  
Thermal Transition ◽  
Scanning Calorimetry ◽  
Helix Structure ◽  
Stabilizing Effect ◽  
Collagen Molecules ◽  
Thermal Stability Of

Abstract In this communication, sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen were studied. We used ultrasensitive differential scanning calorimetry (US-DSC) to directly monitor the thermal transition of collagen in the presence of SDS. The results show that SDS affects the conformation and thermal stability of collagen very differently depending on its concentrations. At CSDS ≤ 0.05 mM, the enhanced thermal stability of collagen indicates the stabilizing effect by SDS. However, a further increase of SDS leads to the denaturation of collagen, verifying the well-known ability of SDS to unfold proteins. This striking difference in thermodynamics and conformational changes of collagen caused by SDS concentrations can be explained in terms of their interactions. With increasing SDS, the binding of SDS to collagen can be dominated by electrostatic interaction shifting to hydrophobic interaction, and the latter plays a key role in loosening and unfolding the triple-helix structure of collagen. The important finding in the present study is the stabilizing effect of SDS on collagen molecules at extreme low concentration. Graphical abstract

scholarly journals Properties Change of Korean Traditional Animal Glue Depending on The Parts of Cattle Hide and Extraction Conditions

2021 ◽  
Vol 37 (5) ◽  
pp. 557-566
Author(s):  
Gyu Hyuk Cho ◽  
Ji Sun Choi ◽  
Dea Woo Park ◽  
Han Hyoung Lee ◽  
Yong Jea Chung
Keyword(s):  
Molecular Weight ◽  
Triple Helix ◽  
Average Molecular Weight ◽  
Extraction Time ◽  
Animal Glue ◽  
Helix Structure ◽  
Average Change ◽  
Total Molecular Weight ◽  
Different Parts ◽  
Over Time

We investigated the properties of Korean traditional animal glue which are associated with the use of different parts of cattle hide and extraction conditions. Both average molecular weight(Mw, Mz) and polydispersity (PDI) of the animal glue increased with extraction time, whereas only PDI decreased after 48h. There were no differences in the average molecular weight and PDI for the different cattle hide parts used, although a individual difference was observed with regard to total molecular weight. Differences in extracts over time were compared by investigating the amide regions representing the gelatien component of the animal glue. The triple helix structure of the belly skin deteriorated in a manner proportional to the extraction time, and differences were observed for each cattle hide part. The yellowness increased with the extraction time; however, the viscosity was not proportional to the average change in molecular weight. This study has some limitations because of difficulties in the quality control of cases where small amounts of glue were extracted as small differences might impact the overall results considerably. Further research exploring various extraction conditions is required to ensure the prodiction of traditional animal glue with optimum qualities.

scholarly journals The Characteristics of Intrinsic Fluorescence of Type I Collagen Influenced by Collagenase I

2018 ◽  
Vol 8 (10) ◽  
pp. 1947 ◽  
Author(s):  
Yiming Shen ◽  
Deyi Zhu ◽  
Wenhui Lu ◽  
Bing Liu ◽  
Yanchun Li ◽  
...  
Keyword(s):  
Fluorescence Intensity ◽  
Self Assembly ◽  
Triple Helix ◽  
Type I Collagen ◽  
Intrinsic Fluorescence ◽  
Type I ◽  
Food And Agriculture ◽  
Mechanism Research ◽  
Helix Structure ◽  
Assembly Behavior

The triple helix structure of collagen can be degraded by collagenase. In this study, we explored how the intrinsic fluorescence of type I collagen was influenced by collagenase I. We found that tyrosine was the main factor that could successfully excite the collagen fluorescence. Initially, self-assembly behavior of collagen resulted in a large amount of tyrosine wrapped with collagen, which decreased the fluorescence intensity of type I collagen. After collagenase cleavage, some wrapped-tyrosine could be exposed and thereby the intrinsic fluorescence intensity of collagen increased. By observation and analysis, the influence of collagenase to intrinsic fluorescence of collagen was investigated and elaborated. Furthermore, collagenase cleavage to the special triple helix structure of collagen would result in a slight improvement of collagen thermostability, which was explained by the increasing amount of terminal peptides. These results are helpful and effective for reaction mechanism research related to collagen, which can be observed by fluorescent technology. Meantime, the reaction behaviors of both collagenase and collagenolytic proteases can also be analyzed by fluorescent technology. In conclusion, this research provides a foundation for the further investigation of collagen reactions in different areas, such as medicine, nutrition, food and agriculture.

Triple Helix, Quadruple Helix and Quintuple Helix and How Do Knowledge, Innovation and the Environment Relate to Each Other?

2012 ◽  
pp. 29-59
Author(s):  
Elias Carayannis ◽  
David F.J. Campbell
Keyword(s):  
Sustainable Development ◽  
Triple Helix ◽  
Social Ecology ◽  
Quadruple Helix ◽  
Natural Environments ◽  
Structure Model ◽  
Triple Helix Model ◽  
Knowledge Innovation ◽  
Quintuple Helix ◽  
Helix Structure

This article develops an inter-disciplinary and trans-disciplinary framework of analysis that relates knowledge, innovation and the environment (natural environments) to each other. For that purpose the five-helix structure model of the Quintuple Helix is being introduced. The Triple Helix model, designed by Etzkowitz and Leydesdorff (2000), focuses on the relations of universities, industry and governments. The Quadruple Helix (Carayannis & Campbell, 2009) blends in the perspective of a media-based and culture-based public. The Quintuple Helix finally frames knowledge and innovation in the context of the environment (natural environments). Therefore, the Quintuple Helix can be interpreted as an approach in line with sustainable development and social ecology. “Eco-innovation” and “eco-entrepreneurship” should be processed in such a broader understanding of knowledge and innovation.

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