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출처: 이북나라 전자책 『U. Protein structure and function』 1쪽 · 6쪽 · 10쪽 · 15쪽 · 19쪽 · 24쪽. 원문에 없는 주제·저자·발행일은 넣지 않았습니다.

U. Protein structure and function

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The activation of glycerol dehydrogenase by ppGpp Huyen Nga Hoang, Thanh Tuyen Tran, and Che-Hun Jung Department of Molecular Medicine, Department of Chemistry Graduate school, Chonnam National University, Gwangju, Korea ABSTRACT Glycerol dehydrogenase (GldA) from Escherichia coli is a Zn2 -containing alcohol dehydrogenase which catalyzes the NAD -dependent oxidation of glycerol to + + dihydroxyacetone. In this study, ppGpp binds to GldA and activates its activity with the half maximal activation at 33.1 ± 3.1 μM.

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[U. Protein structure and function-3] Malate Dehydrogenase a novel ppGpp binding protein Rana Aqeel Afzal1, Che-Hun Jung1 1Molecular Medicine, Chonnam National University, Gwangju 61186, Korea The citric acid cycle is the central oxidative pathway in prokaryotes and eukaryotes under aerobic conditions. One of the reactions in the cycle is the conversion of malate to oxaloacetate, catalyzed by NAD+- or NADP+-dependent malate dehydrogenase (MDH).

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[U. Protein structure and function-5] Solution structure of the nucleotide hydrolase BlsM: importance of its substrate specificity Minhee Kang1 ̇2, Zhengrong Wu1 ̇* 1Chemistry, The Ohio State University, Columbus 43212, USA, 2Pharmacy, Korea University, Sejong 30019, S. Korea Biosynthesis of the peptidyl nucleoside antifungal agent blasticidin S in Streptomyces griseochromogenes requires the hydrolytic function of a nucleotide N-glycosidase, BlsM, to provide free cytosine from CMP.

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Purification and protein interaction of weak binding human chromatin remodeling component by crosslinking experiments Gye-young Park, Jeongmin Han, Jae-Hyun Park, Ji-Hye Yun, Weontae Lee * Structural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of life Science & Biotechnology, Yonsei University, Seoul, 120-749, Korea. ABSTRACT To accomplish viral life cycle, HIV virus hijacks host proteins, the so-called co-factors of replication.

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The Dynamic Structure of human Interleukin 33 in the apo form Se-Young Son , Sang-Hyun Son , Young-Ha Ryu and Young Ho Jeon 1,2 1 Allercuris Co. Ltd., Lab.402, College of Pharmacy, Sejong-ro 2511, Sejong 30019, Korea, 2 College of Pharmacy, Korea University, Sejong-ro 2511, Sejong 30019, Korea I. ABSTRACT COMPARISON BETWEEN FREE FORM AND BINDING FORMS (red) IL-33 (PDB ID : 4KC3) Interleukin 33 (IL33) is a member of IL1 family that drives production of T Site2 (plum) ST2 helper-2 (Th2) associated cytokines as well as plays a critical role in the Site1 development of allergic diseases such as…

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[U. Protein structure and function-18] The RING domain of mitochondrial E3 ubiquitin ligase 1 and its complex with Ube2D2: crystallization and X-ray diffraction Sang-Ok Lee1 ̇2 ̇#, Chong-Kil Lee2, Kyoung-Seok Ryu3 ̇4 ̇*, Seung-Wook Chi1 ̇5 ̇* 1Disease Target Structure Research Center, Division of Biomedical Research , KRIBB, Daejeon 34141, Republic of Korea, 2College of Pharmacy, Chungbuk National University, Cheongju 28644, Republic of Korea, 3Protein Structure Research Group, Korea Basic Science Institute, Cheongju-si 28119, Republic of Korea, 4Department of Bio- Analytical Science, KBSI…

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