Hydrogen-Bond-Regulated Distinct Functional-Group Display at the Inner and Outer Wall of Vesicles

2015 ◽  
Vol 127 (23) ◽  
pp. 6859-6864 ◽  
Author(s):  
Amrita Sikder ◽  
Anindita Das ◽  
Suhrit Ghosh
Keyword(s):  
Hydrogen Bond ◽  
Functional Group ◽  
Outer Wall

Hydrogen-Bond-Regulated Distinct Functional-Group Display at the Inner and Outer Wall of Vesicles

2015 ◽  
Vol 54 (23) ◽  
pp. 6755-6760 ◽  
Author(s):  
Amrita Sikder ◽  
Anindita Das ◽  
Suhrit Ghosh
Keyword(s):  
Hydrogen Bond ◽  
Functional Group ◽  
Outer Wall

Hydrogen Bond-Accelerated meta-Selective C–H Borylation of Aromatic Compounds and Expression of Functional Group and Substrate Specificities

ACS Catalysis ◽  
2019 ◽  
Vol 9 (3) ◽  
pp. 1705-1709 ◽  
Author(s):  
Xu Lu ◽  
Yusuke Yoshigoe ◽  
Haruka Ida ◽  
Mitsumi Nishi ◽  
Motomu Kanai ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Aromatic Compounds ◽  
Functional Group ◽  
Substrate Specificities

scholarly journals Endogenous Binding of Steroid Molecules to DNA Nucleotides by a Ca2+/PO4- Process to Enable Gene Transcription

2020 ◽  
Author(s):  
Charles Schaper
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonds ◽  
Ligand Binding ◽  
Gene Transcription ◽  
Functional Group ◽  
Ring Structure ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Steroid Molecule ◽  
First Time

Steroid hormones, such as cortisol, testosterone and estrogen, have powerful control over human physiology, growth, and reproduction, but efforts to deploy its potential, such as with glucocorticoids, a first-line defense of inflammation, are often met with severe side effects. Unfortunately, much is unknown about the basic interaction of steroid molecules with DNA, including its receptors, activators, factors, and the gene transcription procedure. In this research article, a remarkable finding is shown for the first time, in which it is illustrated through structural analysis that the base pairings of the four DNA nucleotides, adenine with thymine (A-T) and cytosine with guanine (C-G), form perfectly the classic four ring structure of the steroid molecule, which indicates the profound result put forth in this article that steroid molecules bind directly to DNA for the purpose of gene transcription. Further, critical to a basic understanding of DNA, it is resolved here of the location of the unusual ``missing" hydrogen bond of the A-T pairing, which has only two internal hydrogen bonds whereas C-G has three hydrogen bonds. It is shown that the third hydrogen bond for A-T is formed when the A-T nucleotide is coupled with corticosteroids, such as cortisol, which has an oxygen functional group that is perfectly positioned to form a hydrogen bond with the accessible oxygen-based functional group of thymine. In addition, to facilitate the binding process, it is shown that Ca2+ ions, which are associated with the ligand binding domain of the steroid receptor prior to its association with DNA, couple the oxygen-based functional groups at each end of the steroid molecule with the PO4- ions of adjacent nucleotides and thus bind the steroid molecule directly to the nucleic acid. The results are further amplified by analysis of the cortisol hormone and the ligand binding domain of the glucocorticoid receptor in its interaction with the A-T nucleotide pairing.

scholarly journals Endogenous Binding of Steroid Molecules to DNA Nucleotides by a Ca2+/PO4- Process to Enable Gene Transcription

2020 ◽  
Author(s):  
Charles Schaper
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonds ◽  
Ligand Binding ◽  
Gene Transcription ◽  
Functional Group ◽  
Ring Structure ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Steroid Molecule ◽  
Transcription Process

Steroid hormones, such as cortisol, testosterone and estrogen, have powerful control over human physiology, growth, and reproduction, but efforts to deploy its potential, such as with glucocorticoids, a first-line defense of inflammation, are often met with severe side effects. Unfortunately, much is unknown about the basic interaction of steroid molecules with DNA, including its receptors, activators, factors, and the gene transcription procedure. In this research article, a remarkable finding is shown for the first time, in which it is illustrated through structural analysis that the base pairings of the four DNA nucleotides, adenine with thymine (A-T) and cytosine with guanine (C-G), form perfectly the classic four ring structure of the steroid molecule, which indicates the profound result put forth in this article that steroid molecules bind directly to DNA for the purpose of gene transcription. Further, critical to a basic understanding of DNA, it is resolved here of the location of the unusual ``missing" hydrogen bond of the A-T and T-A pairings, which has only two internal hydrogen bonds whereas C-G and G-C have three hydrogen bonds. It is shown that the third hydrogen bond for A-T and T-A is formed when the A-T and T-A nucleotides are coupled with corticosteroids, such as cortisol, which has an oxygen functional group that is perfectly positioned to form a hydrogen bond with the accessible oxygen-based functional group of thymine. In addition, to facilitate the binding process, it is shown that Ca$^{2+}$ ions, which are associated with the ligand binding domain of the steroid receptor prior to its association with DNA, couple the oxygen-based functional groups at each end of the steroid molecule with the PO$_4^-$ ions of adjacent nucleotides and thus bind the steroid molecule directly to the nucleic acid. Additionally, the basis of initiating the transcription process is described in which the energy stabilization due to the binding of the ion-steroid complex to DNA is dissipated through the DNA molecule to initiate strand separation locally by increasing the length of hydrogen bonds, thus allowing RNA polymerase action. The results are further amplified by analysis of the cortisol hormone and the ligand binding domain of the glucocorticoid receptor in its interaction with the A-T nucleotide pairing.

5-(5-Ethyl-1,3,4-thiadiazol-2-ylaminomethylene)-2,2-dimethyl-1,3-dioxane- 4,6-dione

2006 ◽  
Vol 62 (4) ◽  
pp. o1520-o1521 ◽  
Author(s):  
Luiz Everson da Silva ◽  
Antonio Carlos Joussef ◽  
Carla Regina Andrighetti-Fröhner ◽  
Cláudia Maria Olivra Simões ◽  
Adailton José Bortoluzzi
Keyword(s):  
Hydrogen Bond ◽  
Carbonyl Group ◽  
Title Compound ◽  
Functional Group ◽  
Chair Conformation ◽  
Membered Ring ◽  
Intramolecular Contact ◽  
Compound C ◽  
Thiadiazole Ring

In the title compound, C11H13N3O4S, the thiadiazole ring is nearly planar, while the 1,3-dioxane-4,6-dione ring exhibits a half-chair conformation. The NH group makes one intramolecular contact with a carbonyl group, forming a six-membered ring. The same functional group is involved in an intermolecular N—H...N hydrogen bond.

CF2H, a Functional Group-Dependent Hydrogen-Bond Donor: Is It a More or Less Lipophilic Bioisostere of OH, SH, and CH3?

2019 ◽  
Vol 62 (11) ◽  
pp. 5628-5637 ◽  
Author(s):  
Yossi Zafrani ◽  
Gali Sod-Moriah ◽  
Dina Yeffet ◽  
Anat Berliner ◽  
Dafna Amir ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Functional Group ◽  
Hydrogen Bond Donor

Assembly, growth and nonlinear thermo-optical properties of nitropeptides

2015 ◽  
Vol 17 (26) ◽  
pp. 16983-16990 ◽  
Author(s):  
Santu Bera ◽  
Deepak K. S. Ambast ◽  
Bipul Pal ◽  
Debasish Haldar
Keyword(s):  
Hydrogen Bond ◽  
Optical Properties ◽  
Phase Modulation ◽  
Functional Group ◽  
Self Phase Modulation ◽  
Π Stacking ◽  
Backbone Conformation

Irrespective of having the same functional group, π-conjugated system, chirality and backbone conformation as nitropeptides 1 and 3, nitropeptide 2 that forms a hydrogen bond and π–π stacking assisted dimer exhibits self-phase modulation.

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