Thermodynamic destabilization of azurin by four different tetramethylguanidinium amino acid ionic liquids.

Amino Acids / chemistry Anions / chemistry Azurin / chemistry Cations / chemistry Entropy Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Imidazoles / chemistry Ionic Liquids / chemistry Methylguanidine / analogs & derivatives Molecular Dynamics Simulation Protein Stability Protein Structure, Secondary Protein Unfolding Transition Temperature
Ionic liquids Molecular dynamics Thermodynamic stability

Journal

International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578

Informations de publication

Date de publication:
01 Jun 2021
Historique:
received: 08 02 2021
revised: 15 03 2021
accepted: 15 03 2021
pubmed: 22 3 2021
medline: 27 7 2021
entrez: 21 3 2021
Statut: ppublish

Résumé

The thermal unfolding of the copper redox protein azurin was studied in the presence of four different amino acid-based ionic liquids (ILs), all of which have tetramethylguanidium as cation. The anionic amino acid includes two with alcohol side chains, serine and threonine, and two with carboxylic acids, aspartate and glutamate. Control experiments showed that amino acids alone do not significantly change protein stability and pH changes anticipated by the amino acid nature have only minor effects on the protein. With the ILs, the protein is destabilized and the melting temperature is decreased. The two ILs with alcohol side chains strongly destabilize the protein while the two ILs with acid side chains have weaker effects. Unfolding enthalpy (ΔH

Identifiants

DOI: 10.1016/j.ijbiomac.2021.03.090 PMID: 33744247
pubmed: 33744247
pii: S0141-8130(21)00608-5
doi: 10.1016/j.ijbiomac.2021.03.090
pii:
doi:

Substances chimiques

Amino Acids 0
Anions 0
Cations 0
Imidazoles 0
Ionic Liquids 0
Azurin 12284-43-4
Methylguanidine 5L0H5Q9VAG
imidazole 7GBN705NH1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

355-364

Informations de copyright

Copyright © 2021 Elsevier B.V. All rights reserved.

Auteurs

Isabella DeStefano (I)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Gabriella DeStefano (G)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Nicholas J Paradis (NJ)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Roshani Patel (R)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Austin K Clark (AK)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Hunter Gogoj (H)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Gurvir Singh (G)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Keertana S Jonnalagadda (KS)

Department of Biological Sciences, Rowan University, Glassboro, NJ 08028, USA; Bantivoglio Honors College, Rowan University, Glassboro, NJ 08028, USA.

Aashka Y Patel (AY)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA.

Chun Wu (C)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA; Department of Molecular and Cellular Biosciences, Rowan University, Glassboro, NJ 08028, USA.

Gregory A Caputo (GA)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA; Department of Molecular and Cellular Biosciences, Rowan University, Glassboro, NJ 08028, USA.

Timothy D Vaden (TD)

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ 08028, USA. Electronic address: vadent@rowan.edu.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Produits chimiques inorganiques › Électrolytes › Ions › Anions › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Métalloprotéines › Azurine › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Produits chimiques inorganiques › Électrolytes › Ions › Cations › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Phénomènes physiques › Thermodynamique › Entropie › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Phénomènes chimiques › Concentration en ions d'hydrogène › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Phénomènes chimiques › Interactions hydrophobes et hydrophiles › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Composés hétérocycliques › Composés hétéromonocycliques › Azoles › Imidazoles › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Actions chimiques et utilisations › Utilisations spécialisées de produits chimiques › Solvants › Liquides ioniques › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Composés chimiques organiques › Amidines › Guanidines › Méthyl-guanidine › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Sciences de l'information › Méthodologies informatiques › Simulation numérique › Simulation de dynamique moléculaire › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Stabilité protéique › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure secondaire des protéines › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Pliage des protéines › Dépliement des protéines › Thermodynamic destabilization of azurin by...
questionsmedicales.fr › Phénomènes physiques › Thermodynamique › Température de transition › Thermodynamic destabilization of azurin by...