ArticleMolecules (Basel, Switzerland)2021
Heat Capacities of l-Histidine, l-Phenylalanine, l-Proline, l-Tryptophan and l-Tyrosine.
Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Physicochemical Characterization of Choline Amino Acid Protic Ionic Liquids as Sustainable Lubricant Candidates.ACS omega · 2026Article
- Antimicrobial Proteinoid Nanostructures via Thermal Condensation of L-Glutamic Acid and L-Tyrosine.Nanomaterials (Basel, Switzerland) · 2025Article
- Preliminary Exploration on the Regulatory Mechanism of Ionic Strength on Conformation and Hydration of Silver Carp Myosin.Foods (Basel, Switzerland) · 2025Article
- Heat Capacities of α-, β-, and γ- Polymorphs of Glycine.Molecules (Basel, Switzerland) · 2024Article
- Amorphous Solid Forms of Ranolazine and Tryptophan and Their Relaxation to Metastable Polymorphs.Crystal growth & design · 2023Article
- Heat Capacities ofMolecules (Basel, Switzerland) · 2023Article
- Heat Capacities of L-Cysteine, L-Serine, L-Threonine, L-Lysine, and L-Methionine.Molecules (Basel, Switzerland) · 2023Article
- Effect of Danhong injection on heart failure in rats evaluated by metabolomics.Frontiers in medicine · 2023Article
- Formation of a Stable Co-Amorphous System for a Brick Dust Molecule by Utilizing Sodium Taurocholate with High Glass Transition Temperature.Pharmaceutics · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In an effort to establish reliable thermodynamic data for proteinogenic amino acids, heat capacities for l-histidine (CAS RN: 71-00-1), l-phenylalanine (CAS RN: 63-91-2), l-proline (CAS RN: 147-85-3), l-tryptophan (CAS RN: 73-22-3), and l-tyrosine (CAS RN: 60-18-4) were measured over a wide temperature range. Prior to heat capacity measurements, thermogravimetric analysis was performed to determine the decomposition temperatures while X-ray powder diffraction (XRPD) and heat-flux differential scanning calorimetry (DSC) were used to identify the initial crystal structures and their possible transformations. Crystal heat capacities of all five amino acids were measured by Tian-Calvet calorimetry in the temperature interval from 262 to 358 K and by power compensation DSC in the temperature interval from 307 to 437 K. Experimental values determined in this work were then combined with the literature data obtained by adiabatic calorimetry. Low temperature heat capacities of l-histidine, for which no literature data were available, were determined in this work using the relaxation (heat pulse) calorimetry from 2 K. As a result, isobaric crystal heat capacities and standard thermodynamic functions up to 430 K for all five crystalline amino acids were developed.
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