The solubilities of five cyclic dipeptides in water and in aqueous urea at 298.15 K: a quantitative model for the denaturation of proteins in aqueous urea solutions.

No abstract is available for this paper.

• Publication year

  1994

• Venue

  Biophysical Chemistry

• Publication date

  1994-09-01

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1016/0301-4622(94)00067-0PMID 7948713
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Peptide-urea interactions as observed in diketopiperazine-urea cocrystal.

  1993cited by this paper
• Urea-diketopiperazine interactions: a model for urea induced denaturation of proteins.

  1993cited by this paper
• A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures.

  1990cited by this paper
• Thermodynamics of dissolution of solid cyclic dipeptides containing hydrophobic side groups

  1989cited by this paper
• Stability of protein structure and hydrophobic interaction.

  1988cited by this paper
• Effects of urea and guanidine hydrochloride on peptide and nonpolar groups.

  1984cited by this paper
• The nature of the accessible and buried surfaces in proteins.

  1976cited by this paper
• Thermodynamic investigations of proteins. III. Thermodynamic description of lysozyme.

  1976cited by this paper
• Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin.

  1974cited by this paper
• [Thermodynamics of hydrophobic interaction in the systems water + glycin + urea and water + alanin + urea at 25 degrees C (author's transl)].

  1973cited by this paper
• Effect of Pressure on the Solubility of Diketopiperazine in Water

  1970cited by this paper
• THE EFFECT OF COMPOUNDS OF THE UREA-GUANIDINIUM CLASS ON THE ACTIVITY COEFFICIENT OF ACETYLTETRAGLYCINE ETHYL ESTER AND RELATED COMPOUNDS.

  1965cited by this paper
• THE THERMODYNAMICS OF THE TERNARY SYSTEM: UREA-SODIUM CHLORIDE-WATER AT 25

  1963cited by this paper
• THE SOLUBILITY OF AMINO ACIDS AND RELATED COMPOUNDS IN AQUEOUS UREA SOLUTIONS.

  1963cited by this paper
• SOLUBILITY OF DIKETOPIPERAZINE IN AQUEOUS SOLUTIONS OF UREA1

  1961cited by this paper

• Thermodynamics, Experimental, and Modelling of Aqueous Electrolyte and Amino Acid Solutions

  2016cites this paper
• A Comprehensive Experimental Study to Understand the Hofmeister Series of Anions of Aqueous Imidazolium-Based Ionic Liquids on Glycine Peptides

  2014cites this paper
• Volumetric, Acoustic, and Refractometric Study of Cyclic Alanylalanine in Aqueous Cobalt Chloride Solutions at Temperatures T = (293.15 to 313.15) K

  2013cites this paper
• Structural basis for the enhanced stability of protein model compounds and peptide backbone unit in ammonium ionic liquids.

  2012cites this paper
• Thermodynamic characterization of the biocompatible ionic liquid effects on protein model compounds and their functional groups.

  2011cites this paper
• The Properties, Formation, and Biological Activity of 2,5-Diketopiperazines

  2010cites this paper
• Effect of osmolyte or GdnHCl on volumetric properties of aqueous solutions containing cyclic dipeptides

  2008cites this paper
• Thermodynamic characterization of the osmolyte effect on protein stability and the effect of GdnHCl on the protein denatured state.

  2007cites this paper
• Trimethylamine N-oxide counteracts the denaturing effects of urea or GdnHCl on protein denatured state.

  2007cites this paper
• The biological activity of the histidine-containing diketopiperazines cyclo(His-Ala) and cyclo(His-Gly).

  2006cites this paper
• An investigation into the biological activity of the selected histidine‐containing diketopiperazines cyclo(His‐Phe) and cyclo(His‐Tyr)

  2004cites this paper
• Densities and solubilities of glycylglycine and glycyl-l-alanine in aqueous electrolyte solutions

  2004cites this paper
• Thermodynamics of protein model compounds: apparent molar volumes and isobaric heat capacities of selected cyclic dipeptides and their transfer properties from water to aqueous urea solutions at T = 298.15 K

  2003cites this paper
• Thermal and urea-induced unfolding of the marginally stable lac repressor DNA-binding domain: a model system for analysis of solute effects on protein processes.

  2003cites this paper
• Thermodynamics, Experimental, and Modelling of Aqueous Electrolyte and Amino Acid Solutions

  2001cites this paper
• Molecular dynamics study on hydrophobic effects in aqueous urea solutions.

  2001cites this paper
• Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: Interpretation of urea and guanidinium chloride m‐values and their correlation with changes in accessible surface area (ASA) using preferential interaction coefficients and the local‐bulk domain mode

  2000cites this paper
• Thermodynamics of Protein Model Compounds: Apparent and Partial Molar Heat Capacities and Volumes of Several Cyclic Dipeptides in Water

  2000cites this paper
• Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect

  1998cites this paper
• Calorimetrically-derived parameters for protein interactions with urea and guanidine-HCl are not consistent with denaturant m values.

  1997cites this paper
• Interactions of α-chymotrypsinogen A with alkylureas

  1996cites this paper
• Interactions of alpha-chymotrypsinogen A with alkylureas.

  1996cites this paper
• Thermodynamics of denaturation of α-chymotrypsinogen A in aqueous urea and alkylurea solutions

  1995cites this paper