Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori
- H. Hemmi, J. Ishibashi, S. Hara, M. Yamakawa
- ChemistryFEBS Letters
- 8 May 2002
Isolation, gene expression and solution structure of a novel moricin analogue, antibacterial peptide from a lepidopteran insect, Spodoptera litura.
- Y. Oizumi, H. Hemmi, M. Minami, A. Asaoka, M. Yamakawa
- BiologyBiochimica et Biophysica Acta
- 31 August 2005
Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata.
- H. Hemmi, T. Kumazaki, Yuji Kobayashi
- Chemistry, BiologyBiochemistry
- 22 June 2005
The CSH motif-containing derivative of AEI (AEI analogue) was chemically synthesized and exhibited unexpected strong inhibition toward Streptomyces griseus protease B (SGPB), while the AEI analogue scarcely inhibited porcine pancreatic elastase (PPE), even though it exhibited almost the same potent inhibitory activity toward SGPB.
Solution structure of the toluene 4-monooxygenase effector protein (T4moD).
The specificity of T4moD as an effector protein was investigated by replacing it in reconstituted T4MO complexes with effector proteins from monooxygenases from other bacterial species by refined through simulated annealing by molecular dynamics in torsion angle space.
Isolation and structure determination of a new antibacterial peptide pentaminomycin C from Streptomyces cacaoi subsp. cacaoi
- I. Kaweewan, H. Hemmi, H. Komaki, S. Kodani
- Chemistry, BiologyJournal of antibiotics (Tokyo. )
- 10 January 2020
A new antibacterial peptide named pentaminomycin C was isolated from an extract of Streptomyces cacaoi NBRC 12748T along with a known peptide BE-18257A, and exhibited antibacterial activities against Gram-positive bacteria including Micrococcus luteus, Bacillus subtilis, and Staphylococcus aureus.
Interaction between the heme and a G-quartet in a heme-DNA complex.
- Kaori Saito, H. Tai, H. Hemmi, N. Kobayashi, Yasuhiko Yamamoto
- ChemistryInorganic Chemistry
- 25 July 2012
The structure of a complex between heme(Fe(3+)) and a parallel G-quadruplex DNA formed from a single repeat sequence of the human telomere, d(TTAGGG), has been characterized by (1)H NMR and provides new insights as to the design of the molecular architecture and functional properties of various heme-DNA complexes.
Structure determination of a siderophore peucechelin from Streptomyces peucetius
- S. Kodani, H. Komaki, Masahiro Suzuki, Fumiya Kobayakawa, H. Hemmi
- Chemistry, BiologyBiometals
- 18 June 2015
Comparison of the biosynthetic genes of structurally related siderophores peucechelin and foroxymithine was accomplished in discussion because the similar genes were found in the genome data of S. venezuelae and S. purpureus.
NMR Detection and Characterization of I-quartets in Parallel DNA Quadruplexes
- Masashi Kinoshita, Shunsuke Takaya, Tomokazu Shibata, H. Hemmi, Yasuhiko Yamamoto
- Chemistry
- 30 May 2015
Four inosine bases (Is) can be cyclically and planarly associated through four hydrogen bonds to form a macrocycle called an I-quartet, in a manner similar to that of the well-known guanine (G)-one...
Internal Hollows in Cooked Rice Grains (Oryza sativa cv. Koshihikari) Observed by NMR Micro Imaging
- A. Horigane, H. Toyoshima, H. Hemmi, W. Engelaar, A. Okubo, T. Nagata
- Materials Science
- 1999
Nondestructive analysis of water distribution and structural changes in cooked rice grains, Oryza sativa cv Koshihikari, was performed with Nuclear Magnetic Resonance (NMR) Micro imaging of protons (…
Local conformational transition of Hydrogenobacter thermophilus cytochrome c552 relevant to its redox potential.
- S. Takayama, Yo-ta Takahashi, K. Akasaka
- Chemistry, BiologyBiochemistry
- 21 July 2007
The present study demonstrated the importance of the structural and dynamic properties of the polypeptide chain in close proximity to the heme for redox regulation of the protein.
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