Malmö University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Hydration of Lysozyme Studied by Raman Spectroscopy
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).ORCID iD: 0000-0002-9852-5440
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
Show others and affiliations
2013 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 117, no 17, p. 4981-4992Article in journal (Refereed)
Abstract [en]

Hydration plays a fundamental role in maintaining the three-dimensional structure and function of proteins. In this study, Raman spectroscopy was used to probe the hydration induced structural changes at various sites of lysozyme under isothermal conditions in the range of water contents from 0 to 44 wt %. Raman hydration curves were constructed from detailed analysis of marker bands. Transition inflection points (wm) and onsets determined from the hydration curves have shown that structural changes start at 7–10 and end at about 35 wt % water. The onset of structural changes coincides with the onset of the broad glass transition earlier observed in this system. The increase of α-helix content starts at very low concentrations of water with wm = 12 wt %. Monitoring the development of importance for enzymatic action hydrophobic clusters has revealed wm = 15 wt % and completion of the process at 25 wt %. The parameters of 621 cm–1 (Phe) and 1448 cm–1 (CH2 bending) modes were found to be sensitive to hydration, suggesting changes in organization of water molecules near the protein surface. The native structure of lysozyme was achieved at 35 wt % water where its content is high enough for filling the space between lysozyme molecules.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2013. Vol. 117, no 17, p. 4981-4992
Keywords [en]
Lysozyme, Sorption Calorimetry, Hydration, Spectroscopy, Glass transition
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:mau:diva-14679DOI: 10.1021/jp4017954ISI: 000318536700027PubMedID: 23557185Scopus ID: 2-s2.0-84877032969Local ID: 16447OAI: oai:DiVA.org:mau-14679DiVA, id: diva2:1418200
Available from: 2020-03-30 Created: 2020-03-30 Last updated: 2024-02-05Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopushttp://pubs.acs.org/doi/abs/10.1021/jp4017954

Authority records

Kocherbitov, VitalyBarauskas, Justas

Search in DiVA

By author/editor
Kocherbitov, VitalyBarauskas, Justas
By organisation
Department of Biomedical Science (BMV)
In the same journal
Journal of Physical Chemistry B
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 75 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf