CuI-Catalyzed Azide–Alkyne Intramoleculari-to-(i+4) Side-Chain-to-Side-Chain Cyclization Promotes the Formation of Helix-Like Secondary Structures

2010 ◽  
Vol 2010 (3) ◽  
pp. 446-457 ◽  
Author(s):  
Mario Scrima ◽  
Alexandra Le Chevalier-Isaad ◽  
Paolo Rovero ◽  
Anna Maria Papini ◽  
Michael Chorev ◽  
...  
Keyword(s):  
Secondary Structures ◽  
Side Chain

scholarly journals Role of Side Chain Size in the Formation of Secondary Structures in Model Peptides

2015 ◽  
Vol 108 (2) ◽  
pp. 519a
Author(s):  
Farbod Mahmoudinobar ◽  
Cristiano L. Dias ◽  
Ronen Zangi
Keyword(s):  
Secondary Structures ◽  
Side Chain ◽  
Model Peptides

scholarly journals Twists or turns: stabilising alpha vs. beta turns in tetrapeptides

2019 ◽  
Vol 10 (45) ◽  
pp. 10595-10600
Author(s):  
Huy N. Hoang ◽  
Timothy A. Hill ◽  
Gloria Ruiz-Gómez ◽  
Frederik Diness ◽  
Jody M. Mason ◽  
...  
Keyword(s):  
Secondary Structures ◽  
Side Chain ◽  
Ring Size ◽  
Beta Turns

Twisting or turning peptides: ring size and chi angle in side chain cross-linked tetrapeptides together control α- or β-turn structures, which mimic irregular secondary structures in proteins.

scholarly journals 2StrucCompare: a webserver for visualizing small but noteworthy differences between protein tertiary structures through interrogation of the secondary structure content

2019 ◽  
Vol 47 (W1) ◽  
pp. W477-W481 ◽  
Author(s):  
Elliot D Drew ◽  
Robert W Janes
Keyword(s):  
Secondary Structure ◽  
Protein Structures ◽  
Secondary Structures ◽  
Residue Level ◽  
Side Chain ◽  
Related Protein ◽  
Tertiary Structures ◽  
Secondary Structure Content ◽  
Protein Secondary Structures

Abstract 2StrucCompare is a webserver whose primary aim is to visualize subtle but functionally important differences between two related protein structures, either of the same protein or related homologues, with similar or functionally different tertiary structures. At the heart of the package is identifying and visualizing differences between conformations at the secondary structure and at the residue level, such as contact differences or side chain conformational differences found between two protein chains. The protein secondary structures are determined according to four established methods (DSSP, STRIDE, P-SEA and STICKS), and as each employs different assignment strategies, small conformational differences between the two structures can give rise to paired residues being denoted as having different secondary structure features with the different methods. 2StrucCompare captures both the large and more subtle differences found between structures, enabling visualization of these differences that could be key to an understanding of a proteins’ function. 2StrucCompare is freely accessible at http://2struccompare.cryst.bbk.ac.uk/index.php

scholarly journals 1P-047 Roles of side-chain packing in the formation of secondary structures of a protein(Protein:Property, The 47th Annual Meeting of the Biophysical Society of Japan)

2009 ◽  
Vol 49 (supplement) ◽  
pp. S70
Author(s):  
Satoshi Yasuda ◽  
Ryota Kodama ◽  
Takashi Yoshidome ◽  
Yuichi Harano ◽  
Masahiro Kinoshita
Keyword(s):  
Annual Meeting ◽  
Secondary Structures ◽  
Side Chain ◽  
Chain Packing ◽  
Biophysical Society ◽  
Side Chain Packing

scholarly journals Effects of side-chain packing on the formation of secondary structures in protein folding

2010 ◽  
Vol 132 (6) ◽  
pp. 065105 ◽  
Author(s):  
Satoshi Yasuda ◽  
Takashi Yoshidome ◽  
Hiraku Oshima ◽  
Ryota Kodama ◽  
Yuichi Harano ◽  
...  
Keyword(s):  
Protein Folding ◽  
Secondary Structures ◽  
Side Chain ◽  
Chain Packing ◽  
Side Chain Packing

Electroluminescent properties of side-chain naphthalimide-derivated polymers

1998 ◽  
Vol 95 (6) ◽  
pp. 1351-1354 ◽  
Author(s):  
C.-M. Bouché ◽  
P. Le Barny ◽  
H. Facoetti ◽  
F. Soyer ◽  
P. Robin
Keyword(s):  
Side Chain
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