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Related Concept Videos

Amino acids03:42

Amino acids

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Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
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Factors Affecting Solubility04:01

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Compared with pure water, the solubility of an ionic compound is less in aqueous solutions containing a common ion (one also produced by dissolution of the ionic compound). This is an example of a phenomenon known as the common ion effect, which is a consequence of the law of mass action that may be explained using Le Chȃtelier’s principle. Consider the dissolution of silver iodide:
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Amino Acid Biosynthetic Pathways01:29

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Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
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Solubility of Ionic Compounds02:55

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Solubility is the measure of the maximum amount of solute that can be dissolved in a given quantity of solvent at a given temperature and pressure. Solubility is usually measured in molarity (M) or moles per liter (mol/L). A compound is termed soluble if it dissolves in water.
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Physical Properties Affecting Solubility02:19

Physical Properties Affecting Solubility

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Solutions of Gases in Liquids
As for any solution, the solubility of a gas in a liquid is affected by the attractive intermolecular forces between solute and solvent species. Unlike solid and liquid solutes, however, there is no solute-solute intermolecular attraction to overcome when a gaseous solute dissolves in a liquid solvent since the atoms or molecules comprising a gas are far separated and experience negligible interactions. Consequently, solute-solvent interactions are the sole...
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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Computational analysis of the amino acid interactions that promote or decrease protein solubility.

Qingzhen Hou1, Raphaël Bourgeas1, Fabrizio Pucci1

  • 1Department of BioModeling BioInformatics & BioProcesses, Université Libre de Bruxelles, Brussels, 1050, Belgium.

Scientific Reports
|October 4, 2018
PubMed
Summary
This summary is machine-generated.

Protein solubility, crucial for function, was studied using statistical potentials. Specific amino acid interactions, like Lys-containing salt bridges, promote solubility, while π-electron interactions favor aggregation.

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Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
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Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Science

Background:

  • Protein solubility is a fundamental biophysical property essential for protein function.
  • Understanding factors influencing protein solubility is key for protein engineering and drug design.

Purpose of the Study:

  • To investigate the relationship between protein solubility and structural/energetic properties.
  • To identify specific amino acid interactions that promote or hinder protein solubility.
  • To develop a computational method for predicting protein solubility.

Main Methods:

  • Utilized statistical potential formalism with two datasets of soluble and aggregation-prone proteins.
  • Computed solubility-dependent distance potentials biased by protein solubility.
  • Calculated protein folding free energies using potentials derived from soluble and aggregation-prone proteins.

Main Results:

  • Identified Lys-containing salt bridges and aliphatic interactions as solubility promoters.
  • Found that aromatic, His-π, cation-π, amino-π, and anion-π interactions reduce solubility.
  • Demonstrated that the difference in folding free energies correlates better with solubility than protein length, isoelectric point, or aliphatic index.

Conclusions:

  • In silico analysis reveals specific residue-residue interactions impact protein solubility.
  • Interactions involving delocalized π-electrons tend to favor aggregation.
  • Findings offer insights for rational protein design to modulate solubility.