Template-Induced Screw Motions within an Aromatic Amide Foldamer Double Helix

Yann Ferrand; Quan Gan; Brice Kauffmann; Hua Jiang; Ivan Huc

doi:10.1002/ange.201101697

Template-Induced Screw Motions within an Aromatic Amide Foldamer Double Helix

Angewandte Chemie International Edition ◽

10.1002/anie.201101697 ◽

2011 ◽

Vol 50 (33) ◽

pp. 7572-7575 ◽

Cited By ~ 69

Author(s):

Yann Ferrand ◽

Quan Gan ◽

Brice Kauffmann ◽

Hua Jiang ◽

Ivan Huc

Keyword(s):

Double Helix ◽

Screw Motions ◽

Aromatic Amide

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Protamine-DNA interaction

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081863 ◽

1978 ◽

Vol 36 (2) ◽

pp. 200-201

Author(s):

D.P. Bazett-Jones ◽

F.P. Ottensmeyer

Keyword(s):

Small Volume ◽

Double Helix ◽

Dna Interaction ◽

Dark Field ◽

Sperm Head ◽

Nuclear Proteins ◽

Field Electron Microscopy ◽

Dark Field Electron ◽

Dna Double Helix ◽

Positively Charged

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.

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Electron microscopic assays of restriction endonuclease cutting, exonuclease digestion, and hybridization

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100113317 ◽

1984 ◽

Vol 42 ◽

pp. 686-687

Author(s):

Mark Hannibal ◽

Jacob Varkey ◽

Michael Beer

Keyword(s):

Electron Microscope ◽

Low Temperature ◽

Restriction Endonuclease ◽

Double Helix ◽

Test Material ◽

Electron Microscopic ◽

Exonuclease Iii ◽

Dna Molecule ◽

Linear Molecules ◽

Exonuclease Digestion

Workman and Langmore have recently proposed a procedure for isolating particular chromatin fragments. The method requires restriction endonuclease cutting of the chromatin and a probe, their digestion with two exonucleases which leave complimentary single strand termini and low temperature hybridization of these. We here report simple electron microscopic monitoring of the four reactions involved.Our test material was ϕX-174 RF DNA which is cut once by restriction endonuclease Xho I. The conversion of circles to linear molecules was followed in Kleinschmidt spreads. Plate I shows a circular and a linear DNA molecule. The rate of cutting is shown in Figure 1.After completion of the endonuclease cutting, one portion of the DNA was treated with exonuclease III, an enzyme known to digest the 3' terminals of double helical DNA. Aliquots when examined in the electron microscope reveal a decreasing length of double helix and increasing bushes at the ends.

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MEASUREMENT OF THE UNWINDING FORCE OF A DNA DOUBLE HELIX

Журнал структурной химии ◽

10.15372/jsc20170213 ◽

2017 ◽

Keyword(s):

Double Helix ◽

Dna Double Helix

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DNA Inspirited Rational Construction of Nonconventional Luminophores with Efficient and Color-Tunable Afterglow

10.26434/chemrxiv.11786448 ◽

2020 ◽

Author(s):

Yunzhong Wang ◽

Saixing Tang ◽

Yating Wen ◽

Shuyuan Zheng ◽

Bing Yang ◽

...

Keyword(s):

Rational Design ◽

Room Temperature ◽

Double Helix ◽

Mechanical Grinding ◽

Room Temperature Phosphorescence ◽

Color Tunable ◽

Potential Applications ◽

Rational Construction ◽

Double Helix Structure ◽

Made In

<div>Persistent room-temperature phosphorescence (p-RTP) from pure organics is attractive </div><div>due to its fundamental importance and potential applications in molecular imaging, </div><div>sensing, encryption, anticounterfeiting, etc.1-4 Recently, efforts have been also made in </div><div>obtaining color-tunable p-RTP in aromatic phosphors5 and nonconjugated polymers6,7. </div><div>The origin of color-tunable p-RTP and the rational design of such luminogens, </div><div>particularly those with explicit structure and molecular packing, remain challenging. </div><div>Noteworthily, nonconventional luminophores without significant conjugations generally </div><div>possess excitation-dependent photoluminescence (PL) because of the coexistence of </div><div>diverse clustered chromophores6,8, which strongly implicates the possibility to achieve </div><div>color-tunable p-RTP from their molecular crystals assisted by effective intermolecular </div><div>interactions. Here, inspirited by the highly stable double-helix structure and multiple </div><div>hydrogen bonds in DNA, we reported a series of nonconventional luminophores based on </div><div>hydantoin (HA), which demonstrate excitation-dependent PL and color-tunable p-RTP </div><div>from sky-blue to yellowish-green, accompanying unprecedentedly high PL and p-RTP </div><div>efficiencies of up to 87.5% and 21.8%, respectively. Meanwhile, the p-RTP emissions are </div><div>resistant to vigorous mechanical grinding, with lifetimes of up to 1.74 s. Such robust, </div><div>color-tunable and highly efficient p-RTP render the luminophores promising for varying </div><div>applications. These findings provide mechanism insights into the origin of color-tunable </div><div>p-RTP, and surely advance the exploitation of efficient nonconventional luminophores.</div>

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