All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Drop coating deposition Raman spectroscopy of proteinogenic amino acids compared with their solution and crystalline state

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F17%3A10366915" target="_blank" >RIV/00216208:11320/17:10366915 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.saa.2017.05.043" target="_blank" >http://dx.doi.org/10.1016/j.saa.2017.05.043</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.saa.2017.05.043" target="_blank" >10.1016/j.saa.2017.05.043</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Drop coating deposition Raman spectroscopy of proteinogenic amino acids compared with their solution and crystalline state

  • Original language description

    The Raman spectra of 20 proteinogenic amino acids were recorded in the solution, glass phase (as drop coating deposition Raman (DCDR) samples) and crystalline forms in the wide spectral range of 200-3200 cm(-1). The most apparent spectral differences between the Raman spectra of the crystalline forms, glass phases and aqueous solutions of amino acids were briefly discussed and described in the frame of published works. The possible density dependencies of spectral bands were noted. In some cases, a strong influence of the sample density, as well as of the organization of the water envelope, was observed. The most apparent changes were observed for Ser and Thr. Nevertheless, for the majority of amino acids, the DCDR sample form is an intermediate between the solution and crystalline forms. In contrast, aromatic amino acids have only a small sensitivity to the form of the sample. Our reference set of Raman spectra is useful for revealing discrepancies between the SERS and solid/solution spectra of amino acids. We also found that some previously published Raman spectra of polycrystalline samples resemble glassy state rather than crystalline spectra. Therefore, this reference set of spectra will find application in every branch of Raman spectroscopy where the spectra of biomolecules are collected from coatings.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

    <a href="/en/project/GBP205%2F12%2FG118" target="_blank" >GBP205/12/G118: Nanobiophotonics for future health care</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2017

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy

  • ISSN

    1386-1425

  • e-ISSN

  • Volume of the periodical

    185

  • Issue of the periodical within the volume

    5 October

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    10

  • Pages from-to

    207-216

  • UT code for WoS article

    000405251700028

  • EID of the result in the Scopus database

    2-s2.0-85020007300