Structures of Ovine Corticotropin-Releasing Factor and Its Ala32 Mutant as Studied by CD and NMR Techniques.
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概要
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The corticotropin-releasing factor (CRF) is a 41-amino acid peptide-amide hormone, which mediates a general stress-response. It has been reported that the substitution of His-32 in the ovine CRF (oCRF) with Ala brings about a 4.5-fold increase in activity [Kornreich et al. (1992) J. Med. Chem. 35, 1870-76]. Here, we have determined the secondary structure of this Ala-substituted ovine CRF ([Ala 32] oCRF) and compare it with that of oCRF using circular dichroism (CD) and NMR techniques in trifluoroethanol (TFE) solution, which is known to stabilize the α-helix formation. In contrast to an earlier report, it was observed the α-helical structure extends to the C-terminus of oCRF. By analyzing the C_??_H and NH chemical shifts, the properties of local structures of oCRF were elucidated. The oCRF and [Ala 32] oCRF have stable α-helical structures in the middle region, regardless of pH and temperature, and the α-helix initiation regions of these peptides are stabilized as the pH is decreased. However, the [Ala 32] oCRF has a more stable α-helical structure than oCRF in the vicinity of the substitution region, and it is thought that this is the cause of the increased activity of [Ala 32] oCRF.
- 社団法人 日本生化学会の論文
著者
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Kim Hyoungman
Department Of Biological Sciences Korea Advanced Institute Of Science And Technology
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Ryu Kyoung-seok
Department Of Biological Sciences Korea Advanced Institute Of Science And Technology
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Chi Seung-wook
Department Of Biological Sciences Korea Advanced Institute Of Science And Technology
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Choi Byong-seok
Department Of Chemistry Korea Advanced Institute Of Science And Technology
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Kim Seung-Ho
Protein Engineering Group, Korea Research Institute of Bioscience and Biotechnology
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CHOI Byong-Seok
Department of Chemistry, Korea Advanced Institute of Science and Technology
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