Promotion of 11/9‐helical folding in α/β‐peptides containing β 2 ‐homoalanine residue

2021 ◽  
Author(s):  
Hyerim Yoon ◽  
Jaeyeon Lee ◽  
Philjae Kang ◽  
Soo Hyuk Choi
Keyword(s):  
Helical Folding

Helical Folding in a Helical Channel: Chiroptical Transcription of Helical Information through Chiral Wrapping

2005 ◽  
Vol 117 (44) ◽  
pp. 7467-7470 ◽  
Author(s):  
Takanobu Sanji ◽  
Nobu Kato ◽  
Masako Kato ◽  
Masato Tanaka
Keyword(s):  
Helical Channel ◽  
Helical Folding

Tweezer-type binding cavity formed by the helical folding of a carbazole–pyridine oligomer

2022 ◽  
Author(s):  
Hye Jin Jang ◽  
Seungwon Lee ◽  
Byung Jun An ◽  
Geunmoo Song ◽  
Hae-Geun Jeon ◽  
...  
Keyword(s):  
Dipole Interactions ◽  
Π Stacking ◽  
Binding Cavity ◽  
Helical Folding

We have synthesised a new aromatic foldamer based on the carbazole–pyridine oligomers that adopt helical conformations via dipole-dipole interactions and π-stacking between two ethynyl bond-linked monomers. This foldamer scaffold has...

Cooperative Effect of the Two Hydrogen Bonding Types on 11/9-Helical Folding of α/β-Peptides

2018 ◽  
Vol 39 (2) ◽  
pp. 244-249 ◽  
Author(s):  
Geunhyuk Jang ◽  
Mihye Lee ◽  
Jaeyeon Lee ◽  
Jihyun Shim ◽  
Philjae Kang ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Cooperative Effect ◽  
Helical Folding

scholarly journals Alpha-helical folding of SilE models upon Ag(His)(Met) motif formation

2018 ◽  
Vol 54 (74) ◽  
pp. 10419-10422 ◽  
Author(s):  
Valentin Chabert ◽  
Maggy Hologne ◽  
Olivier Sénèque ◽  
Olivier Walker ◽  
Katharina M. Fromm
Keyword(s):  
Binding Affinities ◽  
System P ◽  
Helical Folding

The first structures and silver binding affinities of SilE key sequences provide insights in the functioning of the Sil system.

Residue Requirements for Helical Folding in Short α/β-Peptides:  Crystallographic Characterization of the 11-Helix in an Optimized Sequence

2005 ◽  
Vol 127 (38) ◽  
pp. 13130-13131 ◽  
Author(s):  
Margaret A. Schmitt ◽  
Soo Hyuk Choi ◽  
Ilia A. Guzei ◽  
Samuel H. Gellman
Keyword(s):  
Helical Folding

Farnesylation of the SNARE Protein Ykt6 Increases Its Stability and Helical Folding

2008 ◽  
Vol 377 (5) ◽  
pp. 1334-1345 ◽  
Author(s):  
Olena Pylypenko ◽  
André Schönichen ◽  
Diana Ludwig ◽  
Christian Ungermann ◽  
Roger S. Goody ◽  
...  
Keyword(s):  
Snare Protein ◽  
Helical Folding

Helical folding in heterogeneous foldamers without inter-residual backbone hydrogen-bonding

2012 ◽  
Vol 48 (71) ◽  
pp. 8922 ◽  
Author(s):  
Gowri Priya ◽  
Amol S. Kotmale ◽  
Rupesh L. Gawade ◽  
Deepti Mishra ◽  
Sourav Pal ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Helical Folding

Helical Folding in a Helical Channel: Chiroptical Transcription of Helical Information through Chiral Wrapping

2005 ◽  
Vol 44 (44) ◽  
pp. 7301-7304 ◽  
Author(s):  
Takanobu Sanji ◽  
Nobu Kato ◽  
Masako Kato ◽  
Masato Tanaka
Keyword(s):  
Helical Channel ◽  
Helical Folding

Selective sulfate binding induces helical folding of an indolocarbazole oligomer in solution and solid state

2010 ◽  
Vol 46 (5) ◽  
pp. 764-766 ◽  
Author(s):  
Jun-il Kim ◽  
Hemraj Juwarker ◽  
Xinfang Liu ◽  
Myoung Soo Lah ◽  
Kyu-Sung Jeong
Keyword(s):  
Solid State ◽  
Helical Folding

The higher order structure of the centromere

Genome ◽  
1987 ◽  
Vol 29 (4) ◽  
pp. 588-593 ◽  
Author(s):  
J. B. Rattner ◽  
C. C. Lin
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Light Microscopy ◽  
Condensation Process ◽  
Order Structure ◽  
Centromere Region ◽  
Key Words Centromere ◽  
Additional Level ◽  
Helical Folding ◽  
Scanning Electron

The architecture of the centromere region of mouse chromosomes has been studied in cells grown in the presence of 5-azacytidine. This drug interferes with normal condensation producing elongated centromere regions. It has been found that this effect is reversible in the presence of the drug, allowing the observation of the repackaging of the extended centromere into a structure exhibiting native centromere morphology. Light microscopy as well as transmission and scanning electron microscopy of this condensation process suggests that the native centromere is formed by the helical folding of a subfiber with an approximate diameter of 100 nm. This fiber is in turn composed of loops of the 30-nm fiber class. The boundary between successive gyres of the subfiber are obscured at the completion of condensation resulting in the formation of a homogenous 250- to 300-nm fiber that is the native centromere. These observations provide evidence for an additional level of chromatin organization within the metaphase chromosome. Key words: centromere, azacytidine.

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