| bHLH | basic helix-loop-helix |
|---|---|
| bHLH-ZIP | basic helix-loop-helix-leucine zipper |
| HLH | helix-loop-helix; hemophagocytic lymphohistiocytosis |
| RPF | relaxed pelvic floor; renal plasma flow; retroperitoneal fibrosis |
| RSTL | relaxed skin tension lines |
| HLH | B)-helix-loop-helix |
|---|---|
| bHLH | Basic Helix-Loop-Helix |
| bHLH | Basic region helix-loop-helix |
| H-T-H | helix-turn-helix |
| HhH | Helix-hairpin-Helix |
| helix loop helix | <molecular biology> A motif associated with transcription factors, allowing them to recognise and bind to specific DNA sequences. Two _ helices are separated by a loop. Examples: myoblast MyoD1, c myc, Drosophila genes daughterless, hairy, twist, scute, achaete, asense. Not the same as helix turn helix. (18 Nov 1997) |
|---|---|
| helix-loop-helix motifs | A group of 20-residue peptides characterised by two alpha helices separated by a non-helical segment. These recurring supersecondary structural patterns are found in many sequence-specific DNA-binding proteins. (12 Dec 1998) |
| helix turn helix | <molecular biology> A motif associated with transcription factors, allowing them to bind to and recognise specific DNA sequences. Two amphipathic _ helices are separated by a short sequence with a _ sheet. One helix lies across the major groove of the DNA, while the recognition helix enters the major groove and interacts with specific bases. An example in Drosophila is the homeotic gene fushi tarazu, that binds to the sequence TCAATTAAATGA. Not the same as helix loop helix. (18 Nov 1997) |
| helix-turn-helix motifs | The first DNA-binding protein motif to be recognised. Helix-turn-helix motifs were originally identified in bacterial proteins but have since been found in hundreds of DNA-binding proteins from both eukaryotes and prokaryotes. They are constructed from two alpha helices connected by a short extended chain of amino acids, which constitute the "turn." the two helices are held at a fixed angle, primarily through interactions between the two helices. (12 Dec 1998) |
| relaxed control | The ability of certain plasmids to continue to replicate after their bacteria stop dividing, theresult is a single bacteria that containshundreds of plasmids. (09 Oct 1997) |
| relaxed DNA | <molecular biology> DNA that isn't supercoiled. (09 Oct 1997) |
| relaxed mutant | A mutant bacterium that continues to synthesise RNA in a medium that lackscertain nutrients or amino acids which that sort of bacterium normallyneeds present before it can make RNA. (09 Oct 1997) |
| relaxed plasmid | A plasmid that replicatesindependently of the main bacterial chromosome and is present in 10-500 copies per cell. (09 Oct 1997) |
| a helix | The helical (commonly right-handed) form present in many proteins, deduced by Pauling and Corey from X-ray diffraction studies of proteins such as alpha-keratin; the helix is stabilised by hydrogen bonds between, e.g., ==C==O and HN== groups (symbolised by the centre dot in ==CO-HN==) of different eupeptide bonds. In a true a helix, there are 3.6 amino acid residues per turn of the helix. Synonym: 3.613 helix, Pauling-Corey helix. Collagen helix, an extended left-handed helix resulting from the high levels of glycine, l-proline, and l-hydroxyproline present in the collagens. There are 3.3 amino acids per turn of the helix. Three of those left-handed helices form a triple superhelix that is right-handed. (05 Mar 2000) |
| alpha helix | <molecular biology> A particular helical folding of the polypeptide backbone in protein molecules (both fibrous and globular), in which the carbonyl oxygens are all hydrogen bonded to amide nitrogen atoms three residues along the chain. The translation of amino acid residues along the long axis is 0.15 nm and the rotation per residue, 100 |
| Pauling-Corey helix | The helical (commonly right-handed) form present in many proteins, deduced by Pauling and Corey from X-ray diffraction studies of proteins such as alpha-keratin; the helix is stabilised by hydrogen bonds between, e.g., ==C==O and HN== groups (symbolised by the centre dot in ==CO-HN==) of different eupeptide bonds. In a true a helix, there are 3.6 amino acid residues per turn of the helix. Synonym: 3.613 helix, Pauling-Corey helix. Collagen helix, an extended left-handed helix resulting from the high levels of glycine, l-proline, and l-hydroxyproline present in the collagens. There are 3.3 amino acids per turn of the helix. Three of those left-handed helices form a triple superhelix that is right-handed. (05 Mar 2000) |
| groove of crus of the helix | A transverse fissure on the cranial surface of the auricle corresponding to the crus of the helix. Synonym: sulcus cruris helicis. (05 Mar 2000) |
| pi helix | A rare right-handed helix found only in small portions of certain proteins. Stabilised by similar hydrogen bonds as in an a helix; there are 4.3 amino acid residues per turn of the helix. (05 Mar 2000) |
| Watson-Crick helix | The helical structure assumed by two strands of deoxyribonucleic acid, held together throughout their length by hydrogen bonds between bases on opposite strands, referred to as Watson-Crick base pairing. See: base pair. Synonym: DNA helix, double helix, twin helix. (05 Mar 2000) |
| muscle of notch of helix | An occasional muscle on the cranial surface of the auricle spanning the antitragohelicine fissure. Synonym: musculus incisurae helicis, musculus intertragicus. (05 Mar 2000) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|