keadilan PATUT DITEGAKKAN ,,
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Monday, August 30, 2010
Wednesday, August 25, 2010
Monday, August 23, 2010
Monday, August 2, 2010
Sunday, August 1, 2010
CREATING GRAPHICAL OBJECT
SUMMARY ON ACD/CHEMSKETCH
ACD/ChemSketch is an integrated software package from Advanced Chemistry Development to help chemists to draw eaasily chemistry struture, reactions and schematic diagram, calculating chemical structures and others. It also includes many structure modes that extend its possibilities.
There are application which are accessible through Acd/ChemSketch; some are ACD/ ChemBasic, ACD/ I-Lab, ACD/ Tautomers which are respectively a special programming language to customize ACD/ Labs software, an interner -basedservice to get instant access to chemical databasesand property perdiction programme.
On the creating graphical object, it shows how to learn to draw a diagram of energy reaction, various type of orbitals, vacuum distillation apparatus, two-chain DNA strand, and lipid and micelles.
In the drawing simple structures, it shows how to draw various atoms bonds, as well as labels and polymers, flip a drawn molecular structure, select, rotate and resize drawn structures, clean the screen and output to file, document and print.
In the drawing more complex structure, it shows how to draw ring structure, delete and replace atoms, set atom's charge, draw cation and anion, specify types of bonds, generate stereo descriptors and change various atomic structure.
CHAPTER 2: DRAWING SIMPLE STRUCTURES
CHAPTER 3: DRAWING MORE COMPLEX STRUCTURES
CHAPTER 9: CREATING GRAPHICAL OBJECT
ENERGY OF REACTION DIAGRAM
ENERGY OF REACTION DIAGRAM
VARIOUS TYPES OF ORBITALS
VACUUM DISTILLATION APPARATUS
A TWO-CHAIN DNA STRAND
LIPIDS AND MICELLES
3 D MaCroMolecULe
Spatial structure of Lch-beta peptide from two-component lantibiotic Lichenicidin VK21
A novel synergetic lantibiotic pair, Lchalpha(3249.51 Da) and Lchbeta(3019.36 Da), termed lichenicidin VK21, was isolated from the producer strain Bacillus licheniformis VK21. Chemical and spatial structures of Lchalphaand Lchbeta were determined. Each peptide contains 31 amino acid residues linked by 4 intramolecular thioether bridges and the N-terminal 2-oxobutyryl group. Spatial structures of Lchalpha and Lchbetawere studied by NMR spectroscopy in methanol solution. Lchalpha peptide displays structural homology with mersacidin-like lantibiotics and involves relatively well-structured N- and C-terminal domains connected by a flexible loop stabilized by thioether bridge Ala11-S-Ala21. In contrast, the Lchbetapeptide represents prolonged hydrophobic alpha-helix flanked with more flexible N- and C-terminal domains. A lantibiotic cluster of the Bacillus licheniformis VK21 genome which comprises the structural genes, lchA1 and lchA2, encoding the lantibiotics precursors, as well as the gene of a modifying enzyme lchM1, was amplified and sequenced. The mature peptides, Lchalphaand Lchbetainteract synergistically to possess antibiotic activity against Gram-positive bacteria within a nanomolar concentration range, though the individual peptides were shown to be active at micromolar concentrations. Our results afford molecular insight into mechanism of lichenicidin VK21 action.
RELATED STRUCTURES
Primary Citation of: 2KTN 2KTO
EXPERIMENTAL DETAILS
Method: Solution NMR
Experimental Data: NMR Restraint Grid
MOLECULAR DESCRIPTION
Classification: Antibiotic
Structure Weight: 3031.56
Molecule: LchB
Polymer: 1
Type: polypeptide (L)
Lenght: 32
Chains: A
SOURCE
Polymer: 1
Scientific Name: Bacillus Licheniformis
RELATED PDB ENTRIES
2ktn: structure of alpha peptide
MODIFIED RESIDUES
PRIMARY CITATION
Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21.
http://www.pdb.org/pdb/explore/explore.do?structureId=2KTO
A novel synergetic lantibiotic pair, Lchalpha(3249.51 Da) and Lchbeta(3019.36 Da), termed lichenicidin VK21, was isolated from the producer strain Bacillus licheniformis VK21. Chemical and spatial structures of Lchalphaand Lchbeta were determined. Each peptide contains 31 amino acid residues linked by 4 intramolecular thioether bridges and the N-terminal 2-oxobutyryl group. Spatial structures of Lchalpha and Lchbetawere studied by NMR spectroscopy in methanol solution. Lchalpha peptide displays structural homology with mersacidin-like lantibiotics and involves relatively well-structured N- and C-terminal domains connected by a flexible loop stabilized by thioether bridge Ala11-S-Ala21. In contrast, the Lchbetapeptide represents prolonged hydrophobic alpha-helix flanked with more flexible N- and C-terminal domains. A lantibiotic cluster of the Bacillus licheniformis VK21 genome which comprises the structural genes, lchA1 and lchA2, encoding the lantibiotics precursors, as well as the gene of a modifying enzyme lchM1, was amplified and sequenced. The mature peptides, Lchalphaand Lchbetainteract synergistically to possess antibiotic activity against Gram-positive bacteria within a nanomolar concentration range, though the individual peptides were shown to be active at micromolar concentrations. Our results afford molecular insight into mechanism of lichenicidin VK21 action.
RELATED STRUCTURES
Primary Citation of: 2KTN 2KTO
EXPERIMENTAL DETAILS
Method: Solution NMR
Experimental Data: NMR Restraint Grid
MOLECULAR DESCRIPTION
Classification: Antibiotic
Structure Weight: 3031.56
Molecule: LchB
Polymer: 1
Type: polypeptide (L)
Lenght: 32
Chains: A
SOURCE
Polymer: 1
Scientific Name: Bacillus Licheniformis
RELATED PDB ENTRIES
2ktn: structure of alpha peptide
MODIFIED RESIDUES
| Identifier | Name | Formula | Parent | type |
| 2KT | 2-KETOBUTYRIC ACID | C4 H6 O3 | | nonPolymer |
| DBU | (2E)-2-AMINOBUT-2-ENOIC ACID | C4 H7 N O2 | ALA | glycine |
| DAL | D-ALANINE | C3 H7 N O2 | | dPeptideLinking |
| DBA | 2-AMINO-ACRYLIC ACID | C3 H5 N O2 | ALA | glycine |
| DHB | D-ALPHA-AMINOBUTYRIC ACID | C4 H9 N O2 | | dpeptideLinking |
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