It converts any audio signals on a PC or game console into a 5. 1-channel 16-bit / 48 kHz Dolby Digital format at 640 kbit / s and transports it via a single S / PDIF cable.

It offers increased bitrates ( up to 6. 144 Mbit / s ), support for more audio channels ( up to 13. 1 ), and improved coding techniques ( only at low data rates ) to reduce compression artifacts, enabling lower data rates than those supported by AC-3 ( e. g. 5. 1-channel audio at 256 kbit / s ).

The Audigy could process up to four EAX environments simultaneously with its upgraded on-chip DSP and native EAX 3. 0 ADVANCED HD support, and supported up to 5. 1-channel output.

5. 1, offered 5. 1-channel support which adds a center channel speaker and LFE subwoofer output, most useful for movie watching.

The widely-used 5. 1-channel audio system consists of five full range main ( Left, Center, Right, Left rear Surround, and Right rear Surround ) plus a Low-Frequency Effects ( LFE ) channel.

The basic and most common version of the format is a 5. 1-channel system, similar to a Dolby Digital setup, which encodes the audio as five primary ( full-range ) channels plus a special LFE ( low-frequency effects ) channel for the subwoofer.

* MPEG Multichannel – Backward compatible 5. 1-channel surround sound.

Beginning in the late 1990s, and continuing throughout much of the 2000s, home-theater technology progressed with the development of the DVD-Video format, Dolby Digital 5. 1-channel audio (" surround sound ") speaker systems, and high-definition television ( HDTV ).

In the late 1990s, a new wave of home-cinema interest was sparked by the development of DVD-Video, Dolby Digital and DTS 5. 1-channel audio, and high-quality front video projectors that provide a cinema experience at a price that rivals a big-screen HDTV.

DVD-Audio offers many possible configurations of audio channels, ranging from single-channel mono to 5. 1-channel surround sound, at various sampling frequencies and sample rates.

ATSC also boasts 5. 1-channel surround sound using the Dolby Digital AC-3 format.

The binding of TNF to TNF-R1 has been shown to initiate the pathway that leads to caspase activation via the intermediate membrane proteins TNF receptor-associated death domain ( TRADD ) and Fas-associated death domain protein cIAP1 / 2 inhibit TNF-α signaling by binding to TRAF2.

The protein is organized with 6 transmembrane segments, then the C1 cytoplasmic domain, then another 6 membrane segments, and then a second cytoplasmic domain called C2.

* BAR domain, a protein domain

Bacteria use a primase belonging to the DnaG protein superfamily which contains a catalytic domain of the TOPRIM fold type.

G protein coupled receptors ( GPCRs ), also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein-linked receptors ( GPLR ), comprise a large protein family of transmembrane receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses.

These G proteins are made from three subunits, with the G domain located on the largest one ( the α unit ); together with the two smaller subunits ( β and γ units ), they form a tightly associated protein complex.

An intracellular GPCR domain in turn activates a G protein.

Also known as ionotropic receptors, this group of channels open in response to specific ligand molecules binding to the extracellular domain of the receptor protein.

EPM2A codes for the protein laforin, a dual specificity phosphatase ( DSP ) with a carbohydrate binding domain ( CBM-20 ).

Surprisingly, vertebrates have only one such protein with DSP domain as well as CBM-20 domain.

* Protein module or protein domain

There are a number of conserved regions in the catalytic domain of protein kinases.

The N-terminal transcriptional activation domain contains a large number of phosphorylation sites and can be considered as the primary target for protein kinases transducing stress signals.

The protein kinases that are known to target this transcriptional activation domain of p53 can be roughly divided into two groups.

* RING finger domain, a protein structural domain

Histidine-specific protein kinases are structurally distinct from other protein kinases and are found in prokaryotes, fungi, and plants as part of a two-component signal transduction mechanism: a phosphate group from ATP is first added to a histidine residue within the kinase, then transferred to an aspartate residue on a receiver domain on a different protein or the kinase itself, thus activating the aspartate residue.

Shown is a pyramidal cell | pyramidal neuron from the hippocampus, stained for green fluorescent protein.

This egg ( food ) | egg's albumin | protein has undergone denaturation and loss of solubility, caused by the high rise of the temperature of the egg during the cooking process.

A schematic visual model of oxygen-binding process, showing all four monomer s and heme s, and protein | protein chains only as diagramatic coils, to facilitate visualization into the molecule.

Image: Localisations02eng. jpg | Proteins in different cellular compartments and structures tagged with green fluorescent protein.

A representation of the 3D structure of the protein myoglobin showing turquoise alpha helix | alpha helices.

Resonance ( chemistry ) | Resonance structures of the peptide bond that links individual amino acids to form a protein polymer

The DNA sequence of a gene genetic code | encodes the amino acid sequence of a protein.

Image: PBP catalysis. svg | Penicillin binding protein forming cross-links in newly formed bacterial cell wall.

This protein was the first to have its structure resolved by X-ray crystallography by Max Perutz and John Kendrew | Sir John Cowdery Kendrew in 1958, which led to them receiving a Nobel Prize in Chemistry in 1962.

An example of a Green Fluorescent Protein | GFP fusion protein.

Zhang et al., 2008 SFK: Src Family Kinases | Src family kinases. JIP: MAPK8IP1 | JNK-interacting protein 1

Actin filaments are shown in red, microtubules in green, and the cell nucleus | nuclei are in blue. The cytoskeleton ( also CSK ) is a cellular scaffolding or skeleton contained within a cell's cytoplasm and is made out of protein.

***** Rhinoceros, from: en: Dürer's Rhinoceros | Dürer's woodcutRhinoceroses are odd-toed ungulates with horns made of keratin, the same type of protein composing hair.

Diagram illustrating the disulphide bond s ( red ) that link the Immunoglobulin light chain | light ( green ) and Immunoglobulin heavy chain | heavy ( blue ) protein subunits of Immunoglobulin G ( IgM ) molecules.

Image: C-reactive protein. png | C-reactive protein

This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and John Kendrew | Sir John Cowdery Kendrew in 1958, for which they received a Nobel Prize in Chemistry.

Image: RB1. JPG | Crystal structure of the Retinoblastoma tumour suppressor protein bound to E2F peptide Polymer.

The human cyclophilin family, as represented by the structures of the isomerase protein domain | domain s of some of its members.