Analisis Penerapan Sistem Akuntansi Penjualan Kredit Dan Penerimaan Kas Dalam Mendukung Pengendalian Intern Perusahaan (Studi Kasus PT. Smart Tbk Refinery Surabaya)

System of selling credit accounting and system of cash receiving from account receivable is the source of life to achieving company goals. This research on the system of credit sales and cash receipts to support the company internal control. This research was conducted at PT. SMART Tbk Refinery Surabaya. PT. SMART Tbk Refinery Surabaya only selling cooking oil in the form of branded product and trading product on credit. PT. SMART Tbk Refinery Surabaya still has any weakness on system of selling credit accounting and system of cash receiving from account receivable, some of the sales transaction activity that occurred less supportive of the company\u27s internal control. This study aims to provide information to companies about the advantages and weakness of credit sales accounting system and cash receipts that have been applied by the company

Alphabetical List of Popular Metabolic Pathway Databases.

<p>Alphabetical List of Popular Metabolic Pathway Databases.</p

Alphabetical Listing of Toxic Compound Databases.

<p>Alphabetical Listing of Toxic Compound Databases.</p

Alphabetical List of Metabolomic, Chemical or Spectral Databases.

<p>Alphabetical List of Metabolomic, Chemical or Spectral Databases.</p

A screen shot of DrugBank's SNP-ADR table.

<p>This displays the information on the adverse drug reactions (ADRs) and associated SNP (single nucleotide polymorphisms) with certain drugs and drug targets (<a href="http://www.drugbank.ca" target="_blank">http://www.drugbank.ca</a>).</p

A screenshot montage illustrating the types of viewing and searching options available in HMDB (http://www.hmdb.ca).

<p>A screenshot montage illustrating the types of viewing and searching options available in HMDB (<a href="http://www.hmdb.ca" target="_blank">http://www.hmdb.ca</a>).</p

A Simple Method to Measure Protein Side-Chain Mobility Using NMR Chemical Shifts

Protein side-chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein–protein, protein–DNA, protein–RNA, and protein–cofactor interactions. NMR spectroscopy has long been used to provide insights into the motions of side-chain groups. Currently, the method of choice for studying side-chain dynamics by NMR is the measurement of methyl ²H autorelaxation. Methyl ²H autorelaxation exhibits simple relaxation mechanisms and can be straightforwardly converted to meaningful dynamic parameters. However, methyl groups can only be found in 6 of 19 side-chain bearing amino acids. Consequently, only a sparse assessment of protein side-chain dynamics is possible. Therefore, there is a significant interest in developing novel methods of studying side-chain motions that can be applied to all types of side-chains. Here, we show how side-chain chemical shifts can be used to determine the magnitude of fast side-chain motions in proteins. The chemical shift method is applicable to all side-chain bearing residues and does not require any additional measurements beyond standard NMR experiments for backbone and side-chain assignments

Role of polysaccharide and lipid in lipopolysaccharide induced prion protein conversion

<p>Conversion of native cellular prion protein (PrP^c) from an α-helical structure to a toxic and infectious β-sheet structure (PrP^Sc) is a critical step in the development of prion disease. There are some indications that the formation of PrP^Sc is preceded by a β-sheet rich PrP (PrP^β) form which is non-infectious, but is an intermediate in the formation of infectious PrP^Sc. Furthermore the presence of lipid cofactors is thought to be critical in the formation of both intermediate-PrP^β and lethal, infectious PrP^Sc. We previously discovered that the endotoxin, lipopolysaccharide (LPS), interacts with recombinant PrP^c and induces rapid conformational change to a β-sheet rich structure. This LPS induced PrP^β structure exhibits PrP^Sc-like features including proteinase K (PK) resistance and the capacity to form large oligomers and rod-like fibrils. LPS is a large, complex molecule with lipid, polysaccharide, 2-keto-3-deoxyoctonate (Kdo) and glucosamine components. To learn more about which LPS chemical constituents are critical for binding PrP^c and inducing β-sheet conversion we systematically investigated which chemical components of LPS either bind or induce PrP conversion to PrP^β. We analyzed this PrP conversion using resolution enhanced native acidic gel electrophoresis (RENAGE), tryptophan fluorescence, circular dichroism, electron microscopy and PK resistance. Our results indicate that a minimal version of LPS (called detoxified and partially de-acylated LPS or dLPS) containing a portion of the polysaccharide and a portion of the lipid component is sufficient for PrP conversion. Lipid components, alone, and saccharide components, alone, are insufficient for conversion.</p

RENAGE indicates that shaking recPrP^c generates oligomers.

<p>A PrP PICUP ladder (lane 1) is used to size the oligomers formed by shaking recMoPrP ^90–231 in pH 5.5 buffer at 350 rpm and 37°C for 1 day (lane 2). Shaking-induced oligomers are predominantly a distribution of 8-mers to 13-mers. In comparison oligomers formed in urea and salt exhibit a bimodal size distribution of 7-mers to 12-mers (lane 3). Longer periods of shaking recMoPrP ^90–231 (shaking at 350 rpm, 37°C for 2 days) will also generate a fibril band and bimodal distribution of 8-mers to 12-mers and larger oligomers (>16-mers) (lane 4).</p

Fourier transform infrared spectroscopy shows that shaking-induces conversion to oligomers with increased β-sheet structure, dominated by turns and loops.

<p>A) FTIR of oligomers formed by shaking-induced conversion (at 250 rpm and 37°C) of recMoPrP ^23–231 (black line) is drastically different from monomeric recMoPrP^c^23–231 (grey line). The absorbance spectra are shown in solid lines and the corresponding 2^nd derivative spectra are shown in dashed lines. B) Spectral deconvolution and component analysis of the fibril FTIR spectrum (solid line) is fit with Gaussian peaks to a deconvoluted spectrum (dashed line).</p