A Reverse Turn Structure Induced by ad,l-α-Aminoxy Acid Dimer

2003 ◽  
Vol 125 (47) ◽  
pp. 14452-14457 ◽  
Author(s):  
Dan Yang ◽  
Jin Qu ◽  
Wei Li ◽  
De-Ping Wang ◽  
Yi Ren ◽  
...  
Keyword(s):  
Reverse Turn ◽  
Turn Structure

An Unusual Reverse Turn Structure Adopted by a Furanoid Sugar Amino Acid Incorporated in Gramicidin S

2004 ◽  
Vol 126 (11) ◽  
pp. 3444-3446 ◽  
Author(s):  
Gijsbert M. Grotenbreg ◽  
Mattie S. M. Timmer ◽  
Antonio L. Llamas-Saiz ◽  
Martijn Verdoes ◽  
Gijsbert A. van der Marel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gramicidin S ◽  
Reverse Turn ◽  
Turn Structure

Decoupling of Forward and Reverse Turn-on Threshold Voltages in Schottky-Type p-GaN Gate HEMTs

2021 ◽  
pp. 1-1
Author(s):  
Junting Chen ◽  
Mengyuan Hua ◽  
Chengcai Wang ◽  
Ling Liu ◽  
Lingling Li ◽  
...  
Keyword(s):  
Turn On ◽  
Threshold Voltages ◽  
Reverse Turn ◽  
Schottky Type

An Improved Turn Structure for Inducing β‐Hairpin Formation in Peptides

2021 ◽  
Author(s):  
James S. Nowick ◽  
Xingyue Li ◽  
Andrew L. Sabol ◽  
Michał Wierzbicki ◽  
Patrick J. Salveson
Keyword(s):  
Turn Structure ◽  
Hairpin Formation

Stereochemical Control of Hairpin Formation in β-Peptides Containing Dinipecotic Acid Reverse Turn Segments

2000 ◽  
Vol 122 (17) ◽  
pp. 3995-4004 ◽  
Author(s):  
Yong Jun Chung ◽  
Bayard R. Huck ◽  
Laurie A. Christianson ◽  
Heather E. Stanger ◽  
Susanne Krauthäuser ◽  
...  
Keyword(s):  
Stereochemical Control ◽  
Reverse Turn ◽  
Hairpin Formation

scholarly journals Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 511
Author(s):  
Yu Suzuki ◽  
Takanori Higashi ◽  
Takahiro Yamamoto ◽  
Hideyasu Okamura ◽  
Takehiro K. Sato ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Formic Acid ◽  
Spider Silk ◽  
Chemical Shifts ◽  
Repetitive Sequences ◽  
Silk Protein ◽  
Random Coil ◽  
Oh Groups ◽  
Spider Silk Protein ◽  
Turn Structure

Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated Bombyx mori silk fiber with excellent mechanical properties. To use FA as a spinning solvent for RSP with the sequence of major ampullate spider silk protein from Araneus diadematus, we determined the conformation of RSP in FA using solution NMR to determine the role of FA as a spinning solvent. We assigned 1H, 13C, and 15N chemical shifts to 32-residue repetitive sequences, including polyAla and Gly-rich regions of RSP. Chemical shift evaluation revealed that RSP is in mainly random coil conformation with partially type II β-turn structure in the Gly-Pro-Gly-X motifs of the Gly-rich region in FA, which was confirmed by the 15N NOE data. In addition, formylation at the Ser OH groups occurred in FA. Furthermore, we evaluated the conformation of the as-cast film of RSP dissolved in FA using solid-state NMR and found that β-sheet structure was predominantly formed.

scholarly journals The molecular recognition of kink-turn structure by the L7Ae class of proteins

RNA ◽  
2013 ◽  
Vol 19 (12) ◽  
pp. 1703-1710 ◽  
Author(s):  
L. Huang ◽  
D. M. J. Lilley
Keyword(s):  
Molecular Recognition ◽  
Turn Structure

Synthesis and conformational studies of a stable peptidomimetic β-hairpin based on a bifunctional diketopiperazine turn inducer

2015 ◽  
Vol 39 (5) ◽  
pp. 3250-3258 ◽  
Author(s):  
Leila Vahdati ◽  
Roberto Fanelli ◽  
Guillaume Bernadat ◽  
Isabelle Correia ◽  
Olivier Lequin ◽  
...  
Keyword(s):  
Conformational Studies ◽  
Reverse Turn

A new β-hairpin mimic foldamer based on the assembly of a reverse turn inducer, a peptidomimetic strand, and a tetrapeptide sequence was prepared, and its conformation in solution was assessed by NMR and computational investigations.

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