ArticlePolymers2022
Effects of the Temperature and Salt Concentration on the Structural Characteristics of the Protein (PDB Code 1BBL).
Article in Polymers, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 14 citations in OpenAlex.
- Coarse-Grained Modeling and Simulation of Multistranded RNA Nanostars.Chem & bio engineering · 2026Article
- Propagation of Photoinduced Electric Field Changes Through Phytochrome and their Impact on Conformational Transitions.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Structural stability of Calmodulin-target peptide complex at different temperatures based on molecular dynamics simulation.BMC chemistry · 2025Article
- The Impact of Temperature and Pressure on the Structural Stability of Solvated Solid-State Conformations ofMaterials (Basel, Switzerland) · 2024Article
- The Effect of β-Sheet Secondary Structure on All-β Proteins by Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2024Article
- Antibacterial Potency of an Active Compound fromMolecules (Basel, Switzerland) · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The effect of the temperature and salt solution on the structural characteristics of the protein 1BBL was investigated by molecular dynamics simulations. The paper presents simulation results regarding the non-bonded energy and the structural stability of the protein immersed in salt solutions with different concentrations and temperatures. Our work demonstrates that the electrostatic potential energy and van der Waals energy of the system show the opposite changes with the influence of the external environment. Since the electrostatic potential energy changes more obviously, it is dominated in the non-bonding interactions. The structural parameters, such as the root mean square deviation and the radius of gyration, increased initially and decreased afterward with the increase of the salt concentration. The protein presented the loose structure with a relative low stability when it was immersed in a monovalent solution with a salt concentration of 0.8 mol/L. The salt concentration corresponding to the maximum value of structural parameters in the monovalent salt solution was double that in the divalent salt solution. It was also concluded that the protein presented a compact and stable structure when immersed in salt solutions with a high concentration of 2.3 mol/L. The analysis of the root mean square deviation and root mean square fluctuation of the protein sample also exhibited that the structural stability and chain flexibility are strongly guided by the effect of the temperature. These conclusions help us to understand the structural characteristics of the protein immersed in the salt solutions with different concentrations and temperatures.
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