caa a22 4500 397557620 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199605 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021334 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021334 A Synthetic Peptide Study on the Molten Globule of α-Lactalbumin [Elektronische Daten] [Akio Shimizu, Masamichi Ikeguchi, Takuji Kobayashi, Shintaro Sugai] We investigated the conformations of peptides that encompass the B helix or C helix region formed in the molten globule of bovine α-lactalbumin to get information on the molecular mechanism that stabilizes the molten globule. The CD spectra show that the isolated B and C helices are intrinsically unstable. The chemical shifts, NOE connectivities, and CD spectrum indicate that no helical structure is induced in the C helix region (86-99) by extending the peptide sequence to include the hydrophobic cluster region (101-107), although the hydrophobic cluster region can be regarded as a possible initiation site for folding of the protein. We also clarified that the isolated B helix (23-34) peptide does not directly interact with the C helix or hydrophobic cluster region. These results suggest that the B and C helices in the molten globule are stabilized by their interaction with other parts of the protein. © by the Journal of Biochemistry Regular Papers nationallicence α-lactalbumin nationallicence helix nationallicence hydrophobic cluster nationallicence molten globule nationallicence peptide nationallicence Shimizu Akio Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut Ikeguchi Masamichi Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut Kobayashi Takuji Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut Sugai Shintaro Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut The Journal of Biochemistry Oxford University Press 119/5(1996-05), 947-952 0021-924X 119:5<947 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021334 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021334 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Shimizu Akio Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut NATIONALLICENCE 700 1- Ikeguchi Masamichi Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut NATIONALLICENCE 700 1- Kobayashi Takuji Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut NATIONALLICENCE 700 1- Sugai Shintaro Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/5(1996-05), 947-952 0021-924X 119:5<947 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford