THz absorption spectroscopy of solvated β-lactoglobulin
The influence of β-lactoglobulin (βLG) on the fast sub-picosecond collective hydration dynamics in the solvent was investigated by THz absorption spectroscopy as a function of pH. It is well-known that a change in pH from pH 6 to pH 8 reversibly opens or closes the binding cavity by a transition of...
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| Veröffentlicht in: | The Journal of chemical physics 2014-12, Vol.141 (22), p.22D534-22D534 |
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| container_end_page | 22D534 |
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| container_issue | 22 |
| container_start_page | 22D534 |
| container_title | The Journal of chemical physics |
| container_volume | 141 |
| creator | Vondracek, Hendrik Dielmann-Gessner, Jessica Lubitz, Wolfgang Knipp, Markus Havenith, Martina |
| description | The influence of β-lactoglobulin (βLG) on the fast sub-picosecond collective hydration dynamics in the solvent was investigated by THz absorption spectroscopy as a function of pH. It is well-known that a change in pH from pH 6 to pH 8 reversibly opens or closes the binding cavity by a transition of the E-F loop. Furthermore, the aggregation of the protein into dimers is affected, which is thought to be triggered by changes in the enzyme's electrostatic potential. Our data reveal that pH has a clear influence on the THz absorption of βLG. We discuss this influence in light of the changes observed in the sub-psec solute/solvent dynamics when probed by THz spectroscopy, which are, in turn, seen to correlate with changes in the pH value. |
| doi_str_mv | 10.1063/1.4903237 |
| format | Article |
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It is well-known that a change in pH from pH 6 to pH 8 reversibly opens or closes the binding cavity by a transition of the E-F loop. Furthermore, the aggregation of the protein into dimers is affected, which is thought to be triggered by changes in the enzyme's electrostatic potential. Our data reveal that pH has a clear influence on the THz absorption of βLG. We discuss this influence in light of the changes observed in the sub-psec solute/solvent dynamics when probed by THz spectroscopy, which are, in turn, seen to correlate with changes in the pH value.</description><identifier>ISSN: 0021-9606</identifier><identifier>EISSN: 1089-7690</identifier><identifier>DOI: 10.1063/1.4903237</identifier><identifier>PMID: 25494805</identifier><language>eng</language><publisher>United States: American Institute of Physics</publisher><subject>Absorption spectroscopy ; Animals ; Cattle ; Dimers ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Lactoglobulin ; Lactoglobulins - chemistry ; Physics ; Proteins ; Solvents ; Spectrum analysis ; Static Electricity ; Terahertz Spectroscopy ; Water - chemistry</subject><ispartof>The Journal of chemical physics, 2014-12, Vol.141 (22), p.22D534-22D534</ispartof><rights>2014 AIP Publishing LLC.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c243t-57e1d5b1d2f790c423d94fc23d95b6c77b3fdd05af10aaee9780af67ab8bc7db3</citedby><cites>FETCH-LOGICAL-c243t-57e1d5b1d2f790c423d94fc23d95b6c77b3fdd05af10aaee9780af67ab8bc7db3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25494805$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vondracek, Hendrik</creatorcontrib><creatorcontrib>Dielmann-Gessner, Jessica</creatorcontrib><creatorcontrib>Lubitz, Wolfgang</creatorcontrib><creatorcontrib>Knipp, Markus</creatorcontrib><creatorcontrib>Havenith, Martina</creatorcontrib><title>THz absorption spectroscopy of solvated β-lactoglobulin</title><title>The Journal of chemical physics</title><addtitle>J Chem Phys</addtitle><description>The influence of β-lactoglobulin (βLG) on the fast sub-picosecond collective hydration dynamics in the solvent was investigated by THz absorption spectroscopy as a function of pH. 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| ispartof | The Journal of chemical physics, 2014-12, Vol.141 (22), p.22D534-22D534 |
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| language | eng |
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| source | MEDLINE; AIP Journals Complete; Alma/SFX Local Collection |
| subjects | Absorption spectroscopy Animals Cattle Dimers Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Lactoglobulin Lactoglobulins - chemistry Physics Proteins Solvents Spectrum analysis Static Electricity Terahertz Spectroscopy Water - chemistry |
| title | THz absorption spectroscopy of solvated β-lactoglobulin |
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