scholarly journals Increasing protein stability by engineering the n → π* interaction at the β-turn

2020 ◽  
Vol 11 (35) ◽  
pp. 9480-9487 ◽  
Author(s):  
Bhavesh Khatri ◽  
Puja Majumder ◽  
Jayashree Nagesh ◽  
Aravind Penmatsa ◽  
Jayanta Chatterjee
Keyword(s):  
Amino Acid ◽  
Protein Stability ◽  
Structural Stability ◽  
Direct Consequence ◽  
Helical Conformation ◽  
Amino Acid Residues ◽  
Π Interactions

Amino acid residues adopt a right-handed α-helical conformation with increasing strength of the n → π* interaction. We also demonstrate a direct consequence of n → π* interactions on enhancing the structural stability of proteins.

The roles of amino acid residues at positions 216 and 219 in the structural stability and metabolic functions of rat cytochrome P450 2D1 and 2D2

2008 ◽  
Vol 172 (1) ◽  
pp. 11-21 ◽  
Author(s):  
Shizuo Narimatsu ◽  
Kimio Kiryu ◽  
Rei Yonemoto ◽  
Manabu Yoshino ◽  
Mitsuko Kobatake ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Amino Acid ◽  
Structural Stability ◽  
Amino Acid Residues ◽  
Metabolic Functions

scholarly journals Amino Acid Residues 68–71 Contribute to Influenza A Virus PB1-F2 Protein Stability and Functions

2017 ◽  
Vol 8 ◽  
Author(s):  
Yi-Ying Cheng ◽  
Shih-Rang Yang ◽  
Ying-Ting Wang ◽  
Yu-Hsin Lin ◽  
Chi-Ju Chen
Keyword(s):  
Amino Acid ◽  
Protein Stability ◽  
Influenza A Virus ◽  
Influenza A ◽  
Amino Acid Residues

scholarly journals Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

2014 ◽  
Vol 10 ◽  
pp. 660-666 ◽  
Author(s):  
Michał Jewgiński ◽  
Joanna Krzciuk-Gula ◽  
Maciej Makowski ◽  
Rafał Latajka ◽  
Paweł Kafarski
Keyword(s):  
Amino Acid ◽  
Nmr Spectroscopy ◽  
Secondary Structure ◽  
Helical Conformation ◽  
Structural Studies ◽  
Amino Acid Residues ◽  
Terminal Position ◽  
Dehydroamino Acid

Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.

scholarly journals Capsid Protein C of Tick-Borne Encephalitis Virus Tolerates Large Internal Deletions and Is a Favorable Target for Attenuation of Virulence

2002 ◽  
Vol 76 (7) ◽  
pp. 3534-3543 ◽  
Author(s):  
Regina M. Kofler ◽  
Franz X. Heinz ◽  
Christian W. Mandl
Keyword(s):  
Amino Acid ◽  
Capsid Protein ◽  
Protein C ◽  
Alpha Helix ◽  
Helical Conformation ◽  
Amino Acid Residues ◽  
Structural Class ◽  
Hydrophobic Domain ◽  
Tick Borne Encephalitis ◽  
Subviral Particles

ABSTRACT Deletions ranging in size from 4 to 21 amino acid residues were introduced into the capsid protein of the flavivirus tick-borne encephalitis (TBE) virus. These deletions incrementally affected a hydrophobic domain which is present at the center of all flavivirus capsid protein sequences and part of which may form an amphipathic alpha-helix. In the context of the full-length TBE genome, the deletions did not measurably affect protein expression and up to a deletion length of 16 amino acid residues, corresponding to almost 17% of mature protein C, viable virus was recovered. This virus was strongly attenuated but highly immunogenic in adult mice, revealing capsid protein C as a new and attractive target for the directed attenuation of flaviviruses. Apparently, the larger deletions interfered with the correct assembly of infectious virus particles, and this disturbance of virion assembly is likely to be the molecular basis of attenuation. However, all of the mutants carrying large deletions produced substantial amounts of subviral particles, which as judged from density gradient analyses were identical to recombinant subviral particles as obtained by the expression of the surface proteins prM and E alone. The structural and functional flexibility of protein C revealed in this study and its predicted largely alpha-helical conformation are reminiscent of capsid proteins of other enveloped viruses, such as alphaviruses (N-terminal domain of the capsid protein), retroviruses, and hepadnaviruses and suggest that all of these may belong to a common structural class, which is fundamentally distinct from the classical β-barrel structures of many icosahedral viral capsids. The possibility of attenuating flaviviruses by disturbing virus assembly and favoring the production of noninfectious but highly immunogenic subviral particles opens up a promising new avenue for the development of live flavivirus vaccines.

scholarly journals The Effect of Interactions between Amino Acid Residues on the Surface and Water Molecules on Protein Stability.

1999 ◽  
Vol 39 (supplement) ◽  
pp. S156
Author(s):  
Jun Funahashi ◽  
Kazufumi Takano ◽  
Yuriko Yamagata ◽  
Katsuhide Yutani
Keyword(s):  
Amino Acid ◽  
Protein Stability ◽  
Water Molecules ◽  
Amino Acid Residues

scholarly journals Stabilization of peptides against proteolysis through disulfide-bridged conjugation with synthetic aromatics

2017 ◽  
Vol 15 (8) ◽  
pp. 1921-1929 ◽  
Author(s):  
Yaqi Chen ◽  
Tao Li ◽  
Jianguo Li ◽  
Shiyan Cheng ◽  
Jinghui Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Amino Acid Residues ◽  
Π Interactions ◽  
Efficient Strategy

We developed an efficient strategy for the stabilization of peptides against proteolysis, which involves noncovalent π–π interactions between aromatic amino acid residues in peptides and synthetic electron-deficient aromatics.

scholarly journals Identification of Amino Acid Residues within the N-Terminal Domain of EspA That Play a Role in EspA Filament Biogenesis and Function

2008 ◽  
Vol 190 (6) ◽  
pp. 2221-2226 ◽  
Author(s):  
Mona P. Singh ◽  
Robert K. Shaw ◽  
Stuart Knutton ◽  
Mark J. Pallen ◽  
Valerie F. Crepin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Protein Stability ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Terminal Region ◽  
Translocator Protein ◽  
Amino Acid Residues ◽  
And Function

ABSTRACT Enteropathogenic Escherichia coli employs a filamentous type III secretion system, made by homopolymerization of the translocator protein EspA. In this study, we have shown that the N-terminal region of EspA has a role in EspA's protein stability, interaction with the CesAB chaperone, and filament biogenesis and function.

The Role of Acidic Amino Acid Residues in the Structural Stability of Snake Cardiotoxins†

Biochemistry ◽  
1996 ◽  
Vol 35 (28) ◽  
pp. 9177-9186 ◽  
Author(s):  
Chien-Min Chiang ◽  
Shou-Lin Chang ◽  
Hai-jui Lin ◽  
Wen-guey Wu
Keyword(s):  
Amino Acid ◽  
Structural Stability ◽  
Amino Acid Residues ◽  
Acidic Amino Acid
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