hmoment |
Periodicities in the polar/apolar character of the amino acid sequence of a protein can be examined by assigning to each residue a numerical hydrophobicity and searching for periodicity in the resulting one-dimensional function. The strength of each periodic component is the quantity that has been termed the hydrophobic moment.
When proteins of known three-dimensional structure are examined, it is found that sequences that form alpha helices tend to have, on average, a strong periodicity in the hydrophobicity of af 3.6 residues, the period of the alpha helix. The angle of rotation per residue in alpha helices is 100 degrees. Similarly, many sequences that form strands of beta sheets tend to have a periodicity in their hydrophobicity of about 2.3 residues, the period typical of beta structure. The angle of rotation per residue in beta sheets is 160 degrees. This means that many protein sequences tend to form the periodic structure that maximizes their amphiphilicity.
The hydrophobic moment is measured within a moving window using the method of Eisenberg et al. The default angle of 100 degrees is used for the alpha-helix results and the default of 160 degrees is used for the beta-sheet results. These angles can be changed if required using the appropriate options.
hmoment can plot two graphs when the option '-double' is given, one for the alpha helix moment and one for the beta sheet moment. Otherwise it just plots the alpha helix moment.
% hmoment tsw:hbb_human Hydrophobic moment calculation Output file [hbb_human.hmoment]: |
Go to the input files for this example
Go to the output files for this example
Standard (Mandatory) qualifiers (* if not always prompted): [-seqall] seqall Sequence database USA * -graph xygraph Graph type * -outfile outfile Output file name Additional (Optional) qualifiers: -window integer Window -aangle integer Alpha helix angle (degrees) -bangle integer Beta sheet angle (degrees) Advanced (Unprompted) qualifiers: -baseline float Graph marker line -plot toggle Produce graphic -double boolean Plot two graphs Associated qualifiers: "-seqall" associated qualifiers -sbegin1 integer Start of each sequence to be used -send1 integer End of each sequence to be used -sreverse1 boolean Reverse (if DNA) -sask1 boolean Ask for begin/end/reverse -snucleotide1 boolean Sequence is nucleotide -sprotein1 boolean Sequence is protein -slower1 boolean Make lower case -supper1 boolean Make upper case -sformat1 string Input sequence format -sdbname1 string Database name -sid1 string Entryname -ufo1 string UFO features -fformat1 string Features format -fopenfile1 string Features file name "-graph" associated qualifiers -gprompt boolean Graph prompting -gtitle string Graph title -gsubtitle string Graph subtitle -gxtitle string Graph x axis title -gytitle string Graph y axis title -goutfile string Output file for non interactive displays -gdirectory string Output directory "-outfile" associated qualifiers -odirectory string Output directory General qualifiers: -auto boolean Turn off prompts -stdout boolean Write standard output -filter boolean Read standard input, write standard output -options boolean Prompt for standard and additional values -debug boolean Write debug output to program.dbg -verbose boolean Report some/full command line options -help boolean Report command line options. More information on associated and general qualifiers can be found with -help -verbose -warning boolean Report warnings -error boolean Report errors -fatal boolean Report fatal errors -die boolean Report deaths |
Standard (Mandatory) qualifiers | Allowed values | Default | |
---|---|---|---|
[-seqall] (Parameter 1) |
Sequence database USA | Readable sequence(s) | Required |
-graph | Graph type | EMBOSS has a list of known devices, including postscript, ps, hpgl, hp7470, hp7580, meta, colourps, cps, xwindows, x11, tektronics, tekt, tek4107t, tek, none, null, text, data, xterm, png, xml | EMBOSS_GRAPHICS value, or x11 |
-outfile | Output file name | Output file | <sequence>.hmoment |
Additional (Optional) qualifiers | Allowed values | Default | |
-window | Window | Any integer value | 10 |
-aangle | Alpha helix angle (degrees) | Any integer value | 100 |
-bangle | Beta sheet angle (degrees) | Any integer value | 160 |
Advanced (Unprompted) qualifiers | Allowed values | Default | |
-baseline | Graph marker line | Any numeric value | 0.35 |
-plot | Produce graphic | Toggle value Yes/No | No |
-double | Plot two graphs | Boolean value Yes/No | No |
ID HBB_HUMAN STANDARD; PRT; 146 AA. AC P02023; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE HEMOGLOBIN BETA CHAIN. GN HBB. OS Homo sapiens (Human), Pan troglodytes (Chimpanzee), and OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE. RC SPECIES=HUMAN; RA BRAUNITZER G., GEHRING-MULLER R., HILSCHMANN N., HILSE K., HOBOM G., RA RUDLOFF V., WITTMANN-LIEBOLD B.; RT "The constitution of normal adult human haemoglobin."; RL Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=HUMAN; RX MEDLINE; 81064667. RA LAWN R.M., EFSTRATIADIS A., O'CONNELL C., MANIATIS T.; RT "The nucleotide sequence of the human beta-globin gene."; RL Cell 21:647-651(1980). RN [3] RP SEQUENCE OF 121-146 FROM N.A. RC SPECIES=HUMAN; RX MEDLINE; 85205333. RA LANG K.M., SPRITZ R.A.; RT "Cloning specific complete polyadenylylated 3'-terminal cDNA RT segments."; RL Gene 33:191-196(1985). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN. RC SPECIES=HUMAN; RX MEDLINE; 76027820. RA FERMI G.; RT "Three-dimensional fourier synthesis of human deoxyhaemoglobin at RT 2.5-A resolution: refinement of the atomic model."; RL J. Mol. Biol. 97:237-256(1975). RN [5] RP SEQUENCE. RC SPECIES=P.TROGLODYTES; RX MEDLINE; 66071496. RA RIFKIN D.B., KONIGSBERG W.; RT "The characterization of the tryptic peptides from the hemoglobin of RT the chimpanzee (Pan troglodytes)."; RL Biochim. Biophys. Acta 104:457-461(1965). RN [6] [Part of this file has been deleted for brevity] FT VARIANT 140 140 A -> T (IN ST JACQUES: O2 AFFINITY UP). FT /FTId=VAR_003081. FT VARIANT 140 140 A -> V (IN PUTTELANGE; POLYCYTHEMIA; FT O2 AFFINITY UP). FT /FTId=VAR_003082. FT VARIANT 141 141 L -> R (IN OLMSTED; UNSTABLE). FT /FTId=VAR_003083. FT VARIANT 142 142 A -> D (IN OHIO; O2 AFFINITY UP). FT /FTId=VAR_003084. FT VARIANT 143 143 H -> D (IN RANCHO MIRAGE). FT /FTId=VAR_003085. FT VARIANT 143 143 H -> Q (IN LITTLE ROCK; O2 AFFINITY UP). FT /FTId=VAR_003086. FT VARIANT 143 143 H -> P (IN SYRACUSE; O2 AFFINITY UP). FT /FTId=VAR_003087. FT VARIANT 143 143 H -> R (IN ABRUZZO; O2 AFFINITY UP). FT /FTId=VAR_003088. FT VARIANT 144 144 K -> E (IN MITO; O2 AFFINITY UP). FT /FTId=VAR_003089. FT VARIANT 145 145 Y -> C (IN RAINIER; O2 AFFINITY UP). FT /FTId=VAR_003090. FT VARIANT 145 145 Y -> H (IN BETHESDA; O2 AFFINITY UP). FT /FTId=VAR_003091. FT VARIANT 146 146 H -> D (IN HIROSHIMA; O2 AFFINITY UP). FT /FTId=VAR_003092. FT VARIANT 146 146 H -> L (IN COWTOWN; O2 AFFINITY UP). FT /FTId=VAR_003093. FT VARIANT 146 146 H -> P (IN YORK; O2 AFFINITY UP). FT /FTId=VAR_003094. FT VARIANT 146 146 H -> Q (IN KODAIRA; O2 AFFINITY UP). FT /FTId=VAR_003095. FT HELIX 5 15 FT TURN 16 17 FT HELIX 20 34 FT HELIX 36 41 FT HELIX 43 45 FT HELIX 51 55 FT TURN 56 56 FT HELIX 58 75 FT TURN 76 77 FT HELIX 78 94 FT TURN 95 96 FT TURN 100 100 FT HELIX 101 121 FT HELIX 124 142 FT TURN 143 144 SQ SEQUENCE 146 AA; 15867 MW; EC9744C9 CRC32; VHLTPEEKSA VTALWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLST PDAVMGNPKV KAHGKKVLGA FSDGLAHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGK EFTPPVQAAY QKVVAGVANA LAHKYH // |
Otherwise it writes out a files containing the two columns separated by space or TAB characters. The first column is the position of the start of the window that the hydrophobic moment was calculated in. The second is the hydrophobic moment ('uH'). (If the option '-double' is given then the beta-sheet angle hydrophobicity is given as a third column.)
HMOMENT of HBB_HUMAN from 1 to 146 Window: 10 Angle: 100 Max uH: 0.714 Position uH 1 0.091 2 0.216 3 0.208 4 0.123 5 0.211 6 0.194 7 0.185 8 0.169 9 0.312 10 0.292 11 0.185 12 0.092 13 0.050 14 0.164 15 0.245 16 0.187 17 0.130 18 0.262 19 0.396 20 0.317 21 0.342 22 0.492 23 0.508 24 0.517 25 0.418 26 0.416 27 0.350 28 0.292 29 0.196 30 0.102 31 0.288 32 0.314 33 0.442 34 0.560 35 0.464 36 0.577 37 0.584 38 0.676 39 0.714 40 0.670 41 0.462 42 0.369 43 0.221 44 0.176 45 0.073 46 0.058 [Part of this file has been deleted for brevity] 87 0.179 88 0.201 89 0.065 90 0.041 91 0.110 92 0.181 93 0.261 94 0.312 95 0.200 96 0.263 97 0.369 98 0.310 99 0.362 100 0.495 101 0.585 102 0.450 103 0.488 104 0.547 105 0.315 106 0.311 107 0.252 108 0.187 109 0.215 110 0.295 111 0.425 112 0.303 113 0.421 114 0.528 115 0.487 116 0.436 117 0.501 118 0.532 119 0.409 120 0.447 121 0.308 122 0.383 123 0.252 124 0.361 125 0.374 126 0.314 127 0.219 128 0.310 129 0.361 130 0.439 131 0.433 132 0.507 133 0.336 134 0.344 135 0.207 136 0.234 137 0.299 |
Program name | Description |
---|---|
garnier | Predicts protein secondary structure |
helixturnhelix | Report nucleic acid binding motifs |
pepcoil | Predicts coiled coil regions |
pepnet | Displays proteins as a helical net |
pepwheel | Shows protein sequences as helices |
tmap | Displays membrane spanning regions |