Heat capacities of l-histidine, l-phenylalanine, l-proline, l-tryptophan and l-tyrosine
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F21%3A43922435" target="_blank" >RIV/60461373:22340/21:43922435 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22810/21:43922435
Result on the web
<a href="https://doi.org/10.3390/molecules26144298" target="_blank" >https://doi.org/10.3390/molecules26144298</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/molecules26144298" target="_blank" >10.3390/molecules26144298</a>
Alternative languages
Result language
angličtina
Original language name
Heat capacities of l-histidine, l-phenylalanine, l-proline, l-tryptophan and l-tyrosine
Original language description
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. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GA19-02889S" target="_blank" >GA19-02889S: Stability of amorphous solid dispersions: Predictions by SAFT equations of state and their experimental verification</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Molecules
ISSN
1420-3049
e-ISSN
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Volume of the periodical
26
Issue of the periodical within the volume
14
Country of publishing house
CH - SWITZERLAND
Number of pages
12
Pages from-to
4298
UT code for WoS article
000676354700001
EID of the result in the Scopus database
2-s2.0-85111077064