On the turn-inducing properties of asparagine: the structuring role of the amide side chain, from isolated model peptides to crystallized proteins

2018 ◽  
Vol 20 (5) ◽  
pp. 3411-3423 ◽  
Author(s):  
S. Habka ◽  
W. Y. Sohn ◽  
V. Vaquero-Vara ◽  
M. Géléoc ◽  
B. Tardivel ◽  
...  

The anchoring properties of an asparagine (Asn) residue to its local backbone environment in turn model peptides is characterized using gas phase laser spectroscopy and compared to crystallized protein structures.

2017 ◽  
Vol 19 (26) ◽  
pp. 17128-17142 ◽  
Author(s):  
Woon Yong Sohn ◽  
Sana Habka ◽  
Eric Gloaguen ◽  
Michel Mons

The presence in crystallized proteins of a local anchoring between the side chain of a His residue, located in the central position of a γ- or β-turn, and its local main chain environment, is assessed by the comparison of protein structures with relevant isolated model peptides.


2015 ◽  
Vol 108 (2) ◽  
pp. 519a
Author(s):  
Farbod Mahmoudinobar ◽  
Cristiano L. Dias ◽  
Ronen Zangi

2020 ◽  
Vol 22 (36) ◽  
pp. 20409-20420 ◽  
Author(s):  
Gildas Goldsztejn ◽  
Venkateswara Rao Mundlapati ◽  
Jérémy Donon ◽  
Benjamin Tardivel ◽  
Eric Gloaguen ◽  
...  

Models of protein chains containing a seleno-cysteine (Sec) residue have been investigated by gas phase laser spectroscopy in order to document the effect of the H-bonding properties of the SeH group in the folding of the Sec side chain, by comparison with recent data on Ser- and Cys-containing sequences.


Author(s):  
Yancho D. Devedjiev

Proteins are dynamic systems and interact with their environment. The analysis of crystal contacts in the most accurately determined protein structures (d< 1.5 Å) reveals that in contrast to current views, static disorder and high side-chain entropy are common in the crystal contact area. These observations challenge the validity of the theory that presumes that the occurrence of well ordered patches of side chains at the surface is an essential prerequisite for a successful crystallization event. The present paper provides evidence in support of the approach for understanding protein crystallization as a process dependent on multiple factors, each with its relative contribution, rather than a phenomenon driven by a few dominant physicochemical characteristics. The role of the molecular shape as a factor in the crystallization of proteins by surface mutagenesis is discussed.


2015 ◽  
Vol 91 (3) ◽  
Author(s):  
Farbod Mahmoudinobar ◽  
Cristiano L. Dias ◽  
Ronen Zangi
Keyword(s):  

2007 ◽  
Vol 118 (3) ◽  
pp. 589-595 ◽  
Author(s):  
Adrià Gil ◽  
Sílvia Simon ◽  
Mariona Sodupe ◽  
Juan Bertran

2005 ◽  
Vol 127 (34) ◽  
pp. 11900-11901 ◽  
Author(s):  
Wutharath Chin ◽  
François Piuzzi ◽  
Jean-Pierre Dognon ◽  
Iliana Dimicoli ◽  
Benjamin Tardivel ◽  
...  

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