Controlling them-Poly(phenylene ethynylene) Helical Cavity Environment: Hydrogen Bond Stabilized Helical Structures

2011 ◽  
Vol 44 (1) ◽  
pp. 60-67 ◽  
Author(s):  
Ha H. Nguyen ◽  
James H. McAliley ◽  
David A. Bruce
Keyword(s):  
Hydrogen Bond ◽  
Phenylene Ethynylene ◽  
Helical Structures

scholarly journals Deciphering Aspartyl Peptide Sweeteners Using the Ultimate Molecular Theory of Sweet Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Hydrogen Bond ◽  
Bitter Taste ◽  
Sweet Taste ◽  
Hydrogen Donor ◽  
Helical Structures ◽  
Hydrogen Acceptor ◽  
Recognition Theory ◽  
Selection For ◽  
First Time ◽  
Alpha Carbon

More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers<br>could not go to public platform until now. The sweet and bitter taste theory is updated and presented in separated papers. 1,2 Under the guidance of the sweet<br>receptor helix recognition theory 1, aspartyl/aminomalonyl peptide sweeteners are deciphered. Here it demonstrates that, this series of sweeteners has a<br>hydrogen-bond type hydrogen donor - hydrogen acceptor DH-B moiety and their DH-B is very special. Their B of the DH-B moiety is an oxygen of the carboxylic<br>group, which is widely accepted one. The DH of the DH-B moiety however is the NH of the aspartyl/aminomalonyl peptide, which is a selection for the first time to<br>the best of my knowledge. Even more unusual, their dynamic action acts through<br>the hydrogen on alpha carbon of aspartyl/aminomalonyl group. The receptor main and side grooves have different space characteristics in accepting sweet<br>molecules’ groups, which is elaborated in this paper. This unprecedented elucidation well explains the aspartyl/aminomalonyl peptide sweeteners’<br>phenomenon and, in return, strongly supports this sweet receptor helix recognition theory.

The hydrogen-bond configuration modulates the energy transfer efficiency in helical protein nanotubes

Nanoscale ◽  
2021 ◽  
Author(s):  
Jinlong He ◽  
Lin Zhang ◽  
Ling Liu
Keyword(s):  
Hydrogen Bond ◽  
Energy Transfer ◽  
Building Blocks ◽  
Energy Transfer Efficiency ◽  
Transfer Efficiency ◽  
Helical Structures ◽  
Helical Protein ◽  
Protein Nanotubes

As fundamental building blocks of proteins, helices take different forms including the 310-, α-, and π-helices that feature distinct H-bond networks. The H-bond connectivity is shown to modulate energy transfer efficiency in protein helical structures.

scholarly journals Deciphering Aspartyl Peptide Sweeteners Using the Ultimate Molecular Theory of Sweet Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Hydrogen Bond ◽  
Bitter Taste ◽  
Sweet Taste ◽  
Hydrogen Donor ◽  
Helical Structures ◽  
Hydrogen Acceptor ◽  
Recognition Theory ◽  
Selection For ◽  
First Time ◽  
Alpha Carbon

More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers<br>could not go to public platform until now. The sweet and bitter taste theory is updated and presented in separated papers. 1,2 Under the guidance of the sweet<br>receptor helix recognition theory 1, aspartyl/aminomalonyl peptide sweeteners are deciphered. Here it demonstrates that, this series of sweeteners has a<br>hydrogen-bond type hydrogen donor - hydrogen acceptor DH-B moiety and their DH-B is very special. Their B of the DH-B moiety is an oxygen of the carboxylic<br>group, which is widely accepted one. The DH of the DH-B moiety however is the NH of the aspartyl/aminomalonyl peptide, which is a selection for the first time to<br>the best of my knowledge. Even more unusual, their dynamic action acts through<br>the hydrogen on alpha carbon of aspartyl/aminomalonyl group. The receptor main and side grooves have different space characteristics in accepting sweet<br>molecules’ groups, which is elaborated in this paper. This unprecedented elucidation well explains the aspartyl/aminomalonyl peptide sweeteners’<br>phenomenon and, in return, strongly supports this sweet receptor helix recognition theory.

Indole-based macrocycles and oligomers binding anions

2008 ◽  
Vol 80 (3) ◽  
pp. 599-608 ◽  
Author(s):  
Jae-min Suk ◽  
Min Kyung Chae ◽  
Nam-Kyun Kim ◽  
Uk-Il Kim ◽  
Kyu-Sung Jeong
Keyword(s):  
Hydrogen Bond ◽  
Binding Affinities ◽  
Binding Modes ◽  
Helical Structures ◽  
Binding Properties ◽  
Molecular Building Block ◽  
Internal Cavities ◽  
Sonogashira Reactions ◽  
Helical Folding ◽  
Hydrogen Bond Donors

Indole-based synthetic receptors which bind anions by multiple hydrogen bonds in organic solvents have been prepared. The biindole scaffold bearing two good hydrogen bond donors of indole NHs has been used as a molecular building block to construct the receptors. Incorporation of more hydrogen bond donors or acceptors increases the binding strength and selectivity toward a specific ion. Two macrocycles having different sizes of the internal cavities have been also synthesized, and their binding properties have been compared. Two macrocycles display distinct binding modes with polyatomic anions such as azide, as unequivocally proven by X-ray crystal structures. Finally, a series of oligoindoles containing four, six, and eight indoles have been prepared by Sonogashira reactions. The oligoindoles fold into helical structures upon binding with chloride. The binding affinities of the oligoindoles with chloride increase with increasing of the chain length, which provides an additional evidence for helical folding of the complexes.

Hydrogen Bond-Stabilized Helix Formation of am-Phenylene Ethynylene Oligomer

2002 ◽  
Vol 4 (26) ◽  
pp. 4663-4666 ◽  
Author(s):  
Jennifer M. Cary ◽  
Jeffrey S. Moore
Keyword(s):  
Hydrogen Bond ◽  
Phenylene Ethynylene ◽  
Helix Formation

Studies of a Defective Measles Virus

1968 ◽  
Vol 26 ◽  
pp. 208-209
Author(s):  
R. M. McCombs ◽  
M. Benyesh-Melnick ◽  
J. P. Brunschwig
Keyword(s):  
Inclusion Bodies ◽  
Measles Virus ◽  
Giant Cells ◽  
Helical Structures ◽  
Thin Sections ◽  
Virus Particles ◽  
Extracellular Virus ◽  
Culture Cells ◽  
Infected Cells ◽  
Eosinophilic Inclusions

Measles virus is an agent that is capable of replicating in a number of different culture cells and generally causes the formation of multinucleated giant cells. As a result of infection, virus is released from the cells into the culture fluids and reinfection can be initiated by this cell-free virus. The extracellular virus has been examined by negative staining with phosphotungstic acid and has been shown to be a rather pleomorphic particle with a diameter of about 140 mμ. However, no such virus particles have been detected in thin sections of the infected cells. Rather, the only virus-induced structures present in the giant cells are eosinophilic inclusions (intracytoplasmic or intranuclear). These inclusion bodies have been shown to contain helical structures, resembling the nucleocapsid observed in negatively stained preparations.

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