• Title/Summary/Keyword: Crystal and molecular structure

Search Result 374, Processing Time 0.024 seconds

Effect of the Molecular Structure of Rubbed Polyimide Films for Surface Liquid Crystal Alignment of Nematic Liquid Crystal (네마틱 백정의 표면 액정 배향에관한 폴리이미드막의 분자 구조의 효과)

  • 서대식
    • Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
    • /
    • 1996.05a
    • /
    • pp.232-234
    • /
    • 1996
  • We have investigated the effect of molecular structure of polymer of rubbed polyimide (PI) films for surface liquid crystal alignment. To obtain surface alignment effect of Polymer molecular structure, we measured the polar (out of plane-tilt) anchoring strength and surface ordering of 5CB on rubbed PI surfaces. We have found that the polar anchoring strength of 5CB is depend on the polymer molecular structure of these unidirectionally rubbed PI surfaces.

  • PDF

Au Thin Film Fabrication of <111> Crystal Structure by Effusion Cell Process (Effusion Cell 방식에 의한 <111> 결정구조의 Au 박막의 제작)

  • Pyo Kyung Soo;Kim Kand Dae;Kim Yong Gu;Song Chung Kun
    • Proceedings of the IEEK Conference
    • /
    • 2004.06b
    • /
    • pp.383-386
    • /
    • 2004
  • The one of important requisites for fabricating molecular electronic device is the single crystal direction of bottom substrate nowadays. [1,2]. We obtain the optimum SAM result when the Au crystal is <111> structure for Self-Assembled molecular. To get the <111> crystal Au, we generally repeat heating and cooling course after evaporating Au [3]. However, we can fabricate <111> crystal Av thin film except post treatment because we simultaneously evaporate and anneal using Effusion Cell. In this paper, we study on thin film growth of <111> crystal Au as bottom electrode which is essential for Self-Assembled molecular by Effusion Cell and analyze crystal structure, thickness, surface conductivity and so on as each process condition.

  • PDF

Use of Molecular Replacement to Determine the Phases of Crystal Structure of Taq DNA Polymerase

  • Kim, Young-Soo;Suh, Se-Won
    • BMB Reports
    • /
    • v.29 no.1
    • /
    • pp.38-44
    • /
    • 1996
  • Taq DNA polymerase from Thermus aquaticus has been shown to be very useful in the polymerase chain reaction method, which is being used for amplifying DNA. Not only does Taq DNA polymerase have high commercial value commercial value for the polymerase chain reaction application, but it is also important in studying DNA replication, because it is apparently an homologue to E. coli DNA polymerase I, which has long been used for DNA replication study (Lawyer et ai., 1993). The crystal structure determination of Taq DNA polymerase was initiated. An X-ray diffraction pattern breaks down a crystal structure into discrete sine waves in a Fourier series. The original shape of a crystal object in terms of electron density may be represented as the sum of those sine waves with varying amplitudes and phases in three dimensions. The molecular replacement method was initially employed to provide phase information for the structure of Taq DNA polymerase. The rotation search using the program MERLOT resulted in a solution peak with 5.4 r.m.s. PC-refinement of the X-PLOR program verified the result and also optimized the orientation angles. Next, the translation search using the X-PLOR program resulted in a unique solution peak with 7.35 r.m.s. In addition, the translation search indicated $P3_121$ to be the true space group out of two possible ones. The phase information from the molecular replacement was useful in the MIR phasing experiment.

  • PDF

Crystal structure of the pretense domain of an ATP-independent heat shock protease HtrA

  • Kim, Dong-Young;Kim, Dong-Ryoung;Ha, Sung-Chul;Neratur K.Lokanath;Hwang, Hye-Yeon;Kim, Kyeong-Kyu
    • Proceedings of the Korea Crystallographic Association Conference
    • /
    • 2002.11a
    • /
    • pp.24-24
    • /
    • 2002
  • HtrA (high temperature requirement A), a periplasmic heat shock protein, is known to have molecular chaperone function at low temperatures and proteolytic activity at elevated temperatures. To investigate the mechanism of functional switch to pretense, we have determined the crystal structure of the N-terminal protease domain (PD) of HtrA from Thermotoga maritima. HtrA PD shares the same fold with chymotrypsin-like serine professes. However, crystal structure suggests that HtrA PD is not an active pretense at current state since its active site is not formed properly and blocked by an additional helical lid. On the surface of the lid, HtrA PD has hydrophobic patches that could be potential substrate binding sites for molecular chaperone activity. Present structure suggests that the activation of the proteolytic function of HtrA PD at elevated temperatures might occur by the conformational change.

  • PDF

The Crystal Structure of L-Leucine Dehydrogenase from Pseudomonas aeruginosa

  • Kim, Seheon;Koh, Seri;Kang, Wonchull;Yang, Jin Kuk
    • Molecules and Cells
    • /
    • v.45 no.7
    • /
    • pp.495-501
    • /
    • 2022
  • Leucine dehydrogenase (LDH, EC 1.4.1.9) catalyzes the reversible deamination of branched-chain L-amino acids to their corresponding keto acids using NAD+ as a cofactor. LDH generally adopts an octameric structure with D4 symmetry, generating a molecular mass of approximately 400 kDa. Here, the crystal structure of the LDH from Pseudomonas aeruginosa (Pa-LDH) was determined at 2.5 Å resolution. Interestingly, the crystal structure shows that the enzyme exists as a dimer with C2 symmetry in a crystal lattice. The dimeric structure was also observed in solution using multiangle light scattering coupled with size-exclusion chromatography. The enzyme assay revealed that the specific activity was maximal at 60℃ and pH 8.5. The kinetic parameters for three different amino acid and the cofactor (NAD+) were determined. The crystal structure represents that the subunit has more compact structure than homologs' structure. In addition, the crystal structure along with sequence alignments indicates a set of non-conserved arginine residues which are important in stability. Subsequent mutation analysis for those residues revealed that the enzyme activity reduced to one third of the wild type. These results provide structural and biochemical insights for its future studies on its application for industrial purposes.

Transition of Silk Fibroin by Enzymatic Reaction (효소반응에 의한 견피브로인의 전이)

  • Kim, Dong-Keon;Choi, Jin-Hub;Konishi, Takashi
    • Journal of Sericultural and Entomological Science
    • /
    • v.39 no.1
    • /
    • pp.73-78
    • /
    • 1997
  • The crystalline fraction of silk fibroin (Fcp) was obtained from the aqueous solution of silk fibroin hydrolyzed by $\alpha$-chymotrypsin. The molecular weight of Fcp was found approximately 7000 by using high speed GPC. On the other hand, a high molecular weight of PIFcp product could be obtained by the reverse reaction of enzymatic proteolysis of Fcp precipitates. Some parts of this PIFcp have the molecular weights of approximately 17000 and 24000. As a result of x-ray diffraction analysis, the crystal structure of Fcp and PIFcp was turned out silk-II type and silk-I type, respectively. Upon the reverse reaction of enzymatic protelysis, the structural transition occured from silk-II type to silk-I type crystal for the most of Fcp precipitates. It was confirmed that PIFcp might be somewhat stable crystal structure of silk-I type according to the thermal analysis as well as x-ray diffraction method.

  • PDF

Molecular and Crystal Structure of' Metalaxyl, $C_{15}H_{21}NO_4$ (Metalaxyl, $C_{15}H_{21}NO_4$의 분자 및 결정구조)

  • Keun Il Park;Young Kie Kim;Sung Il Cho;Man Hyung Yoo
    • Korean Journal of Crystallography
    • /
    • v.13 no.3_4
    • /
    • pp.148-151
    • /
    • 2002
  • The molecular and crystal structure of metalaxyl C/sub15/H/sub21/NO₄, was determined by single crystal x-ray diffraction study. Crystallographic data for, title compound P2₁/c, a=7.849(4) Å, b=13.081(5) Å, c=15.100(3) Å, β=101.8(2)°, V= 1517.6(3) ų, Z=4. The molecular. Structure model was solved by direct method and refined by full-matrix least- squares. The final reliable factor, R, is 0.067 for 1694 independent reflections (F/sub o//sup 2/>4σ(F/sub o//sup 2/)). The molecular structure of title compound shows an intramolecular hydrogen bond: Cl2-Hl2A…O1.

Crystal Structure of cis-(Malonato)[(4R,5R)-4,5-bis(Aminomethyl)-2-Isopropyl-1,3-Dioxolane]Platinum(II), A Potent Anticancer Agent

  • Cho, Sang-Woo;Yongkee Cho;Kim, Dai-Kee;Wanchul Shin
    • Korean Journal of Crystallography
    • /
    • v.11 no.1
    • /
    • pp.22-27
    • /
    • 2000
  • The structure of cis-(malonato)[(4R,5R)-4,5-bis(aminomethyl)-2-isopropyl-1,3-dioxolane]platinum(II) with a potent anticancer activity has been determined by the X-ray crystallographic method. Crystal data are as follows: Pt(C/sub 11/H/sub 20/N₂O/sub 6/), M/sub 4/=471.38, monoclinic, P2₁, a=7.112(1), b=33.615(3), c=7.135(1)Å, β=116.80(1)°, V=1522.6(3)Å, and Z=4. The two independent molecules with very similar structures are approximately related by pseudo two-fold screw axis symmetry, which makes the monolinic cell look like the orthorhombic cell with one molecule in the asymmetric unit and space group C222₁. The crystal packing mode is similar to that of the analogue with the dimethyl substituents instead of the isopropyl group. The Pt atom is coordinate to two O and two N atoms in a square planar structure. The six-membered chelate ring in the leaving ligand assumes a conformation intermediate between the half chair and the boat forms. The seven-membered ring in the carrier ligand assumes a twist-chair conformation and the oxolane ring assumes an envelope conformation. Crystal packing consists of the extensive hydrogen-bonding network in the two-dimensional molecular layers and weak van der Waals interactions between these layers.

  • PDF

Crystal Structure of the Metallo-Endoribonuclease YbeY from Staphylococcus aureus

  • Jinwook Lee;Inseong Jo;Ae-Ran Kwon;Nam-Chul Ha
    • Journal of Microbiology and Biotechnology
    • /
    • v.33 no.1
    • /
    • pp.28-34
    • /
    • 2023
  • Endoribonuclease YbeY is specific to the single-stranded RNA of ribosomal RNAs and small RNAs. This enzyme is essential for the maturation and quality control of ribosomal RNA in a wide range of bacteria and for virulence in some pathogenic bacteria. In this study, we determined the crystal structure of YbeY from Staphylococcus aureus at a resolution of 1.9 Å in the presence of zinc chloride. The structure showed a zinc ion at the active site and two molecules of tricarboxylic acid citrate, which were also derived from the crystallization conditions. Our structure showed the zinc ionbound local environment at the molecular level for the first time. Molecular comparisons were performed between the carboxylic moieties of citrate and the phosphate moiety of the RNA backbone, and a model of YbeY in complex with a single strand of RNA was subsequently constructed. Our findings provide molecular insights into how the YbeY enzyme recognizes singlestranded RNA in bacteria.

The Crystal and Molecular Structure of BENTAZONE, $C_{10}H_{12}N_2O_3S$ (BENTAZONE, $C_{10}H_{12}N_2O_3S$의 결정 및 분자구조)

  • 박권일;조성일
    • Korean Journal of Crystallography
    • /
    • v.8 no.2
    • /
    • pp.144-148
    • /
    • 1997
  • the molecular and crystal 3-dimensional structure of bentazone, C10H12N2O3S, has been determined from single crystal x-ray diffraction study. Crystal system is monoclinic: a=8.7817(9)Å, b=9.6059(9) Å, c=13.574(9) Å, β=97.269(1)', V=1136.1(6)Å, space group : P21/c, z=4. The molecular structure model was solved by direct method and refined by full matrix least squares. The final reliable factor, R, is 0.045 for 1396 independent reflections(Fo2>4σFo2). A molecule has a staggered conformation with thiocarbazin ring and isopropyl functional group and the molecules by hydrogen bonds are cross stacked along the c-axis.

  • PDF