scholarly journals Role of Backbone Hydration and Salt-Bridge Formation in Stability of α-Helix in Solution

2003 ◽  
Vol 85 (5) ◽  
pp. 3187-3193 ◽  
Author(s):  
Tuhin Ghosh ◽  
Shekhar Garde ◽  
Angel E. García
Keyword(s):  
Salt Bridge ◽  
Bridge Formation ◽  
Α Helix

scholarly journals Role of Salt Bridge Formation in Antigen-Antibody Interaction

1996 ◽  
Vol 271 (51) ◽  
pp. 32612-32616 ◽  
Author(s):  
Kouhei Tsumoto ◽  
Kyoko Ogasahara ◽  
Yoshitaka Ueda ◽  
Kimitsuna Watanabe ◽  
Katsuhide Yutani ◽  
...  
Keyword(s):  
Salt Bridge ◽  
Bridge Formation ◽  
Antigen Antibody

scholarly journals The Role of E27-K31 and E56-K10 Salt-Bridge Pairs in the Unfolding Mechanism of the B1 Domain of Protein G

2018 ◽  
Vol 18 (1) ◽  
pp. 186
Author(s):  
Tony Ibnu Sumaryada ◽  
Kania Nur Sawitri ◽  
Setyanto Tri Wahyudi
Keyword(s):  
Tertiary Structure ◽  
Salt Bridge ◽  
Protein G ◽  
Core Collapse ◽  
Hydrophobic Core ◽  
B1 Domain ◽  
Collapse Model ◽  
Α Helix ◽  
Dynamics Simulations

Molecular dynamics simulations of the B1 fragment of protein G (56 residues) have been performed at 325, 350, 375, 400, 450 and 500 K for 10 ns. An analysis of its structural and energetic parameters has indicated that the unfolding process of the GB1 protein begins at 900 ps of a 500-K simulation. The unfolding process is initiated when hydrogen bonds in the hydrophobic core region are broken; it continues with the α-helix transformation into coils and turns and ends with the destruction of the β-hairpins. These unfolding events are consistent with the hybrid model of the protein folding/unfolding mechanism, which is a compromise between the hydrophobic core collapse model and the zipper model. Salt-bridge pairs were found to play an important role in the unfolding process by maintaining the integrity of the tertiary structure of the protein. The breaking (or disappearance) of the salt-bridge pairs E27–K31 (in the α-helix) and E56–K10 (connecting β4 and β1) has resulted in the destruction of secondary structures and indicates the beginning of the unfolding process. Our results also suggest that the unfolding process in this simulation was not a complete denaturation of the protein because some β-hairpins remained

scholarly journals The Role of Salt Bridge Formation in Glucagon: An Experimental and Theoretical Study of Glucagon Analogs and Peptide Fragments of Glucagon

2002 ◽  
Vol 8 (5) ◽  
pp. 251-262 ◽  
Author(s):  
Anne-Marie Sapse ◽  
Robert Rothchild ◽  
Duli C. Jain ◽  
Cecilia G. Unson
Keyword(s):  
Theoretical Study ◽  
Salt Bridge ◽  
Peptide Fragments ◽  
Bridge Formation

scholarly journals Role of salt bridge formation in HyHEl-10 Fv-HEL complex: Based on structural analysis of mutant Fv fragments

1999 ◽  
Vol 39 (supplement) ◽  
pp. S134
Author(s):  
M. Shiroishi ◽  
K. Tsumoto ◽  
H. Kondo ◽  
M. Matsushima ◽  
I. Kumagai
Keyword(s):  
Structural Analysis ◽  
Salt Bridge ◽  
Bridge Formation

scholarly journals Structural and Technological Approach to Reveal the Role of the Lipid Phase in the Formation of Soy Emulsion Gels with Chia Oil

Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 48
Author(s):  
Ana M. Herrero ◽  
Claudia Ruiz-Capillas
Keyword(s):  
Raman Spectroscopy ◽  
Structural Properties ◽  
Structural Changes ◽  
Protein Secondary Structure ◽  
Lipid Phase ◽  
Α Helix ◽  
Β Sheet ◽  
Shed Light ◽  
Chia Oil

Considerable attention has been paid to emulsion gels (EGs) in recent years due to their interesting applications in food. The aim of this work is to shed light on the role played by chia oil in the technological and structural properties of EGs made from soy protein isolates (SPI) and alginate. Two systems were studied: oil-free SPI gels (SPI/G) and the corresponding SPI EGs (SPI/EG) that contain chia oil. The proximate composition, technological properties (syneresis, pH, color and texture) and structural properties using Raman spectroscopy were determined for SPI/G and SPI/EG. No noticeable (p > 0.05) syneresis was observed in either sample. The pH values were similar (p > 0.05) for SPI/G and SPI/EG, but their texture and color differed significantly depending on the presence of chia oil. SPI/EG featured significantly lower redness and more lightness and yellowness and exhibited greater puncture and gel strengths than SPI/G. Raman spectroscopy revealed significant changes in the protein secondary structure, i.e., higher (p < 0.05) α-helix and lower (p < 0.05) β-sheet, turn and unordered structures, after the incorporation of chia oil to form the corresponding SPI/EG. Apparently, there is a correlation between these structural changes and the textural modifications observed.

ALPHA-HELIX FORMATION IN C-PEPTIDE RNASE-A INVESTIGATED BY PARALLEL TEMPERING SIMULATIONS

2007 ◽  
Vol 18 (01) ◽  
pp. 91-98 ◽  
Author(s):  
GÖKHAN GÖKOĞLU ◽  
TARIK ÇELİK
Keyword(s):  
Energy State ◽  
Minimum Energy ◽  
Alpha Helix ◽  
Salt Bridge ◽  
Rnase A ◽  
Parallel Tempering ◽  
Implicit Solvent ◽  
C Peptide ◽  
Helix Formation ◽  
Α Helix

We have performed parallel tempering simulations of a 13-residue peptide fragment of ribonuclease-A, c-peptide, in implicit solvent with constant dielectric permittivity. This peptide has a strong tendency to form α-helical conformations in solvent as suggested by circular dichroism (CD) and nuclear magnetic resonance (NMR) experiments. Our results demonstrate that 5th and 8–12 residues are in the α-helical region of the Ramachandran map for global minimum energy state in solvent environment. Effects of salt bridge formation on stability of α-helix structure are discussed.

scholarly journals The role of context on α-helix stabilization: Host-guest analysis in a mixed background peptide model

1997 ◽  
Vol 6 (6) ◽  
pp. 1264-1272 ◽  
Author(s):  
Jianxin Yang ◽  
Erik J. Spek ◽  
Youxiang Gong ◽  
Hongxing Zhou ◽  
Neville R. Kallenbach
Keyword(s):  
Α Helix
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