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Orientation of polar molecules near charged protein interfaces
We study the orientation of water and urea molecules and protein amide vibrations at aqueous α-lactalbumin and α-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation. We vary the net charge of the protein by changing the pH. We find that the orientation of the w...
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| Published in: | Physical chemistry chemical physics : PCCP 2016-03, Vol.18 (1), p.7414-7418 |
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| Main Authors: | , , |
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| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c408t-5cf779ab390652de5f8c3b223b8ca55df1edaf9b01e977a415472168ff12cb223 |
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| cites | cdi_FETCH-LOGICAL-c408t-5cf779ab390652de5f8c3b223b8ca55df1edaf9b01e977a415472168ff12cb223 |
| container_end_page | 7418 |
| container_issue | 1 |
| container_start_page | 7414 |
| container_title | Physical chemistry chemical physics : PCCP |
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| creator | Strazdaite, Simona Meister, Konrad Bakker, Huib J |
| description | We study the orientation of water and urea molecules and protein amide vibrations at aqueous α-lactalbumin and α-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation. We vary the net charge of the protein by changing the pH. We find that the orientation of the water and urea molecules closely follows the net charge of the protein at the surface of the solution. In contrast, the net orientation of the amide groups of the backbone of the protein is independent of pH. We discuss the implications of these results for the mechanism by which urea denatures proteins.
We study the orientation of water and urea molecules and protein amide vibrations at aqueous α-lactalbumin and α-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation. |
| doi_str_mv | 10.1039/c5cp06372h |
| format | article |
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We study the orientation of water and urea molecules and protein amide vibrations at aqueous α-lactalbumin and α-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation.</description><subject>Amides</subject><subject>Charge</subject><subject>Charging</subject><subject>Orientation</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Urea - chemistry</subject><subject>Ureas</subject><subject>Vibration</subject><subject>Water - chemistry</subject><issn>1463-9076</issn><issn>1463-9084</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqN0c9LwzAUB_AgipvTi3elRxGq-dE0yUWQok4YzIOeS5q-uErb1KQ9-N_b2TmvnvJCPjze-wahc4JvCGbq1nDT4ZQJujlAc5KkLFZYJof7WqQzdBLCB8aYcMKO0YymUknJxRzdrX0Fba_7yrWRs1Hnau2jxtVghhpC1MJ4NRvt36GMOu96qNqoanvwVhsIp-jI6jrA2e5coLfHh9dsGa_WT8_Z_So2CZZ9zI0VQumCKZxyWgK30rCCUlZIozkvLYFSW1VgAkoInRCeCEpSaS2hZusW6GrqO47wOUDo86YKBupat-CGkBOhGBVs3OsfVGBKZILFSK8narwLwYPNO1812n_lBOfbaPOMZy8_0S5HfLnrOxQNlHv6m-UILibgg9m__v0N-waR9H0v</recordid><startdate>20160314</startdate><enddate>20160314</enddate><creator>Strazdaite, Simona</creator><creator>Meister, Konrad</creator><creator>Bakker, Huib J</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20160314</creationdate><title>Orientation of polar molecules near charged protein interfaces</title><author>Strazdaite, Simona ; Meister, Konrad ; Bakker, Huib J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-5cf779ab390652de5f8c3b223b8ca55df1edaf9b01e977a415472168ff12cb223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amides</topic><topic>Charge</topic><topic>Charging</topic><topic>Orientation</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Urea - chemistry</topic><topic>Ureas</topic><topic>Vibration</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Strazdaite, Simona</creatorcontrib><creatorcontrib>Meister, Konrad</creatorcontrib><creatorcontrib>Bakker, Huib J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Physical chemistry chemical physics : PCCP</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Strazdaite, Simona</au><au>Meister, Konrad</au><au>Bakker, Huib J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Orientation of polar molecules near charged protein interfaces</atitle><jtitle>Physical chemistry chemical physics : PCCP</jtitle><addtitle>Phys Chem Chem Phys</addtitle><date>2016-03-14</date><risdate>2016</risdate><volume>18</volume><issue>1</issue><spage>7414</spage><epage>7418</epage><pages>7414-7418</pages><issn>1463-9076</issn><eissn>1463-9084</eissn><abstract>We study the orientation of water and urea molecules and protein amide vibrations at aqueous α-lactalbumin and α-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation. We vary the net charge of the protein by changing the pH. We find that the orientation of the water and urea molecules closely follows the net charge of the protein at the surface of the solution. In contrast, the net orientation of the amide groups of the backbone of the protein is independent of pH. We discuss the implications of these results for the mechanism by which urea denatures proteins.
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| identifier | ISSN: 1463-9076 |
| ispartof | Physical chemistry chemical physics : PCCP, 2016-03, Vol.18 (1), p.7414-7418 |
| issn | 1463-9076 1463-9084 |
| language | eng |
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| source | Royal Society of Chemistry:Jisc Collections:Royal Society of Chemistry Read and Publish 2022-2024 (reading list) |
| subjects | Amides Charge Charging Orientation Proteins Proteins - chemistry Urea - chemistry Ureas Vibration Water - chemistry |
| title | Orientation of polar molecules near charged protein interfaces |
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