Transient Non-Native Helix Formation during the Folding of b-Lactoglobulin
In ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient formation of non-native structures is described using th...
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| Format: | Article |
| Language: | English |
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MDPI AG
2014-02-01
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| Series: | Biomolecules |
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| Online Access: | http://www.mdpi.com/2218-273X/4/1/202 |
| _version_ | 1819146148211851264 |
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| author | Masamichi Ikeguchi |
| author_facet | Masamichi Ikeguchi |
| author_sort | Masamichi Ikeguchi |
| collection | DOAJ |
| description | In ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient formation of non-native structures is described using the non-native helix formation during the folding of b-lactoglobulin as a prominent example. Although b-lactoglobulin is a predominantly b-sheet protein, it has been shown to form non-native helices during the early stage of folding. The location of non-native helices, their stabilization mechanism, and their role in the folding reaction are discussed. |
| first_indexed | 2024-12-22T13:09:19Z |
| format | Article |
| id | doaj.art-fef7f674fdf047c39db65ffa8f8cac51 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-12-22T13:09:19Z |
| publishDate | 2014-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-fef7f674fdf047c39db65ffa8f8cac512022-12-21T18:24:48ZengMDPI AGBiomolecules2218-273X2014-02-014120221610.3390/biom4010202biom4010202Transient Non-Native Helix Formation during the Folding of b-LactoglobulinMasamichi Ikeguchi0Department of Bioinformatics, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, JapanIn ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient formation of non-native structures is described using the non-native helix formation during the folding of b-lactoglobulin as a prominent example. Although b-lactoglobulin is a predominantly b-sheet protein, it has been shown to form non-native helices during the early stage of folding. The location of non-native helices, their stabilization mechanism, and their role in the folding reaction are discussed.http://www.mdpi.com/2218-273X/4/1/202a-helixb-sheetstopped-flowcircular dichroismhydrogen-deuterium exchangemutant protein |
| spellingShingle | Masamichi Ikeguchi Transient Non-Native Helix Formation during the Folding of b-Lactoglobulin Biomolecules a-helix b-sheet stopped-flow circular dichroism hydrogen-deuterium exchange mutant protein |
| title | Transient Non-Native Helix Formation during the Folding of b-Lactoglobulin |
| title_full | Transient Non-Native Helix Formation during the Folding of b-Lactoglobulin |
| title_fullStr | Transient Non-Native Helix Formation during the Folding of b-Lactoglobulin |
| title_full_unstemmed | Transient Non-Native Helix Formation during the Folding of b-Lactoglobulin |
| title_short | Transient Non-Native Helix Formation during the Folding of b-Lactoglobulin |
| title_sort | transient non native helix formation during the folding of b lactoglobulin |
| topic | a-helix b-sheet stopped-flow circular dichroism hydrogen-deuterium exchange mutant protein |
| url | http://www.mdpi.com/2218-273X/4/1/202 |
| work_keys_str_mv | AT masamichiikeguchi transientnonnativehelixformationduringthefoldingofblactoglobulin |