• The Journal of Korean Institute of Communications and Information Sciences
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• v.37C no.10
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• pp.977-985
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• 2012

Recently, many countries have been developing new protocols to improve the performance of tactical ad hoc networks for implementing NCW (Network Centric Warfare). Combat net radio (CNR) networks are the most important communication infra for the ground forces such as infantry of Army. U.S. Army had developed MIL-STD-188-220D that is the Interoperability Standard for DMTDs (Digital Messages Transfer Device Subsystems) for voice and data communication in CNR. MIL-STD-188-220D is a candidate for MAC protocol of TMMR which is next radio and has a few constraints to used in TMMR. NAD (Network Access Delay) defined in MIL-STD-188-220D needs time synchronization to avoid collision. However, it is difficult for time synchronization to fit in multi-hop environment. We suggest the enhanced DAP (Deterministic Adaptable Priority)-NAD to prevent conflicts and decrease delays in multi-hop CNR. Simulation results show that the proposed scheme improves the performance in multi-hop CNR networks.

• The Journal of the Institute of Internet, Broadcasting and Communication
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• v.11 no.1
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• pp.199-204
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• 2011

This paper evaluates on the feasibility of MIL-STD-188-220 protocol as a medium access protocol over WNW(Wideband Network Waveform) by simulating and comparing with IEEE 802.11e-based protocol. WNW is newly designed waveform for next-generation broadband tactical communication system. This paper shows the feasibility of using the MIL-STD-188-220 protocol that shows better performance than IEEE 802.11e-based protocol on the particular environment.

• Journal of Microbiology and Biotechnology
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• v.26 no.2
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• pp.226-232
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• 2016

Dihydrodipicolinate reductase is an enzyme that converts dihydrodipicolinate to tetrahydrodipicolinate using an NAD(P)H cofactor in L-lysine biosynthesis. To increase the understanding of the molecular mechanisms of lysine biosynthesis, we determined the crystal structure of dihydrodipicolinate reductase from Corynebacterium glutamicum (CgDapB). CgDapB functions as a tetramer, and each protomer is composed of two domains, an Nterminal domain and a C-terminal domain. The N-terminal domain mainly contributes to nucleotide binding, whereas the C-terminal domain is involved in substrate binding. We elucidated the mode of cofactor binding to CgDapB by determining the crystal structure of the enzyme in complex with NADP⁺ and found that CgDapB utilizes both NADH and NADPH as cofactors. Moreover, we determined the substrate binding mode of the enzyme based on the coordination mode of two sulfate ions in our structure. Compared with Mycobacterium tuberculosis DapB in complex with its cofactor and inhibitor, we propose that the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme.