Globular–disorder transition in proteins: a compromise between hydrophobic and electrostatic interactions?

2016 ◽  
Vol 18 (33) ◽  
pp. 23207-23214 ◽  
Author(s):  
Anupaul Baruah ◽  
Parbati Biswas
Keyword(s):  
Protein Folding ◽  
Electrostatic Interactions ◽  
Protein Disorder ◽  
Disorder Transition ◽  
P Protein

Protein disorder, like protein folding, satisfies the principle of minimal frustration.

Protein folds: towards understanding folding from inspection of native structures

1995 ◽  
Vol 348 (1323) ◽  
pp. 71-79 ◽  
Keyword(s):  
Protein Folding ◽  
Protein Structure ◽  
Secondary Structure ◽  
Electrostatic Interactions ◽  
Protein Domain ◽  
Major Influence ◽  
Protein Topology ◽  
Protein Folds ◽  
Short Summary ◽  
Folded Proteins

Following a short summary of some of the principal features of folded proteins, the results of two complementary studies of protein structure are presented, the first concerned with the factors which influence secondary structure propensity and the second an analysis of protein topology. In an attempt to deconvolute the physical contributions to secondary structure propensities, we have calculated intrinsic ɸ,ψ propensities, derived from the coil regions of proteins. Comparison of intrinsic ɸ,ψ propensities with their equivalent secondary structure values show correlations for both helix and strand. This suggests that the local dipeptide, steric and electrostatic interactions have a major influence on secondary structure propensity. We then proceed to inspect the distribution of protein domain folds observed to date. Several folds occur very commonly, so that 46% of the current non-homologous database comprises only nine folds. The implications of these results for protein folding are discussed.

scholarly journals Electrostatic interactions in the denatured state ensemble: Their effect upon protein folding and protein stability

2008 ◽  
Vol 469 (1) ◽  
pp. 20-28 ◽  
Author(s):  
Jae-Hyun Cho ◽  
Satoshi Sato ◽  
Jia-Cherng Horng ◽  
Burcu Anil ◽  
Daniel P. Raleigh
Keyword(s):  
Protein Folding ◽  
Protein Stability ◽  
Electrostatic Interactions ◽  
Denatured State ◽  
State Ensemble

Order-disorder transition in Cu2ZnSnS4 solar cells from Monte Carlo simulations

2018 ◽  
Author(s):  
Suzanne Wallace ◽  
Jarvist Frost ◽  
Aron Walsh
Keyword(s):  
Monte Carlo ◽  
Solar Cells ◽  
Electrostatic Interactions ◽  
Dominant Form ◽  
Cation Site ◽  
Disorder Transition ◽  
Photogenerated Electrons ◽  
Earth Abundant ◽  
A Site ◽  
Zn Ions

<pre>Kesterite-structured Cu2ZnSnS4 (CZTS) is an earth-abundant and non-toxic semiconductor that is being studied for use as the absorber layer in thin-film solar cells. Currently, the power-conversion efficiencies of this technology fall short of the requirements for commercialisation. Disorder in the Cu-Zn sub-lattice has been observed and is proposed as one explanation for the shortcomings of CZTS solar cells. Cation site disorder averaged over a macroscopic sample does not provide insights into the microscopic cation distribution that will interact with photogenerated electrons and holes. To provide atomistic insight into Cu-Zn disorder, we have developed a Monte Carlo (MC) model based on pairwise electrostatic interactions. Substitutional disorder amongst Cu and Zn ions in Cu-Zn (001) planes on the 2\textit{c} and 2\textit{d} Wyckoff sites -- 2D disorder -- has been proposed as the dominant form of Cu/Zn disorder in near-stoichiometric crystals. We use our model to study the Cu/Zn order-disorder transition in 2D but also allow Zn to substitute onto the Cu 2\textit{a} site -- 3D disorder -- including Cu-Sn (001) planes. We find that defects are less concentrated in Cu-Sn (001) planes but that Zn ions readily substitute onto the Cu 2\textit{a} site and that the critical temperature is lowered for 3D disorder.</pre>

scholarly journals Order-disorder transition in Cu2ZnSnS4 solar cells from Monte Carlo simulations

2018 ◽  
Author(s):  
Suzanne Wallace ◽  
Jarvist Frost ◽  
Aron Walsh
Keyword(s):  
Monte Carlo ◽  
Solar Cells ◽  
Electrostatic Interactions ◽  
Dominant Form ◽  
Cation Site ◽  
Disorder Transition ◽  
Photogenerated Electrons ◽  
Earth Abundant ◽  
A Site ◽  
Zn Ions

<pre>Kesterite-structured Cu2ZnSnS4 (CZTS) is an earth-abundant and non-toxic semiconductor that is being studied for use as the absorber layer in thin-film solar cells. Currently, the power-conversion efficiencies of this technology fall short of the requirements for commercialisation. Disorder in the Cu-Zn sub-lattice has been observed and is proposed as one explanation for the shortcomings of CZTS solar cells. Cation site disorder averaged over a macroscopic sample does not provide insights into the microscopic cation distribution that will interact with photogenerated electrons and holes. To provide atomistic insight into Cu-Zn disorder, we have developed a Monte Carlo (MC) model based on pairwise electrostatic interactions. Substitutional disorder amongst Cu and Zn ions in Cu-Zn (001) planes on the 2\textit{c} and 2\textit{d} Wyckoff sites -- 2D disorder -- has been proposed as the dominant form of Cu/Zn disorder in near-stoichiometric crystals. We use our model to study the Cu/Zn order-disorder transition in 2D but also allow Zn to substitute onto the Cu 2\textit{a} site -- 3D disorder -- including Cu-Sn (001) planes. We find that defects are less concentrated in Cu-Sn (001) planes but that Zn ions readily substitute onto the Cu 2\textit{a} site and that the critical temperature is lowered for 3D disorder.</pre>

Protein–protein inhibitor designed de novo to target the MEEVD region on the C-terminus of Hsp90 and block co-chaperone activity

2019 ◽  
Vol 55 (6) ◽  
pp. 846-849 ◽  
Author(s):  
Marwa N. Rahimi ◽  
Shelli R. McAlpine
Keyword(s):  
Protein Folding ◽  
Protein Interactions ◽  
Cyclic Peptide ◽  
De Novo ◽  
Protein Inhibitor ◽  
Protein Protein Interactions ◽  
Cellular Functions ◽  
P Protein ◽  
Cellular Environment ◽  
C Terminus

Protein–protein interactions control all cellular functions. The designed cyclic peptide LB76 is shown to disrupt key PPI between Hsp90 and co-chaperones. LB76 binds selectively to Hsp90 in the cellular environment and disrupts Hsp90's protein folding activity.

Direct examination of the relevance for folding, binding and electron transfer of a conserved protein folding intermediate

2017 ◽  
Vol 19 (29) ◽  
pp. 19021-19031 ◽  
Author(s):  
Emilio Lamazares ◽  
Sonia Vega ◽  
Patricia Ferreira ◽  
Milagros Medina ◽  
Juan J. Galano-Frutos ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Protein Folding ◽  
Protein Engineering ◽  
Folding Intermediate ◽  
Direct Examination ◽  
Folding Intermediates ◽  
P Protein

Protein engineering allows testing the role of conserved folding intermediates at the native basins of proteins.

scholarly journals Direct comparison of derivatization strategies for LC-MS/MS analysis of N-glycans

The Analyst ◽  
2017 ◽  
Vol 142 (23) ◽  
pp. 4446-4455 ◽  
Author(s):  
Shiyue Zhou ◽  
Lucas Veillon ◽  
Xue Dong ◽  
Yifan Huang ◽  
Yehia Mechref
Keyword(s):  
Protein Folding ◽  
Protein Glycosylation ◽  
Post Translational Modification ◽  
P Protein ◽  
Ms Analysis ◽  
And Function

Protein glycosylation is a common post-translational modification that has significant impacts on protein folding, lifespan, conformation, distribution and function.

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