| Differences in the structural stability and cooperativity between monomeric variants of natural and <i>de novo</i> Cro proteins revealed by high pressure FTIR spectroscopy. | |
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MedLine Citation:
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PMID: 22482462 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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It is widely accepted that pressure affects the structure and dynamics of proteins; however, the underlying mechanism remains unresolved. Our previous studies have investigated pressure effects on fundamental secondary structural elements using model peptides, because these peptides represent a basis from which to understand pressure effects on more complex structures. The present study targeted monomeric variants of naturally occurring bacteriophage λ Cro (natural Cro) and de novo designed λ Cro (SN4m), which are α + β proteins. The sequence of SN4m is 75% different from natural Cro, but the structures are almost identical. Consequently, a comparison of the folding properties of these proteins is of interest. Pressure- and temperature-variable FTIR spectroscopic analyses revealed that the α-helices and the β-sheets of natural Cro are cooperatively and reversibly unfolded by pressure and temperature, whereas those of SN4m are not cooperatively unfolded by pressure, i.e., the α-helices of SN4m unfold at significantly higher pressure than the β-sheets, and irreversibly unfold by temperature. The higher unfolding pressure for the α-helices of SN4m indicates the presence of an intermediate structure of SN4m that does not retain β-sheet structure but does preserve the α-helices. The present results demonstrate that the α-helices of natural Cro are stabilized by global tertiary contacts among the α-helices and the β-sheets, whereas the α-helices of SN4m are stabilized by local tertiary contacts between the α-helices. |
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Authors:
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Hiroshi Imamura; Yasuhiro Isogai; Minoru Kato |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-4-6 |
Journal Detail:
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Title: Biochemistry Volume: - ISSN: 1520-4995 ISO Abbreviation: - Publication Date: 2012 Apr |
Date Detail:
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Created Date: 2012-4-9 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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