A simple method for predicting transmembrane alpha helices with better accuracy.
The prediction of a protein's structure from its amino acid sequence has been a long-standing goal of molecular biology. In this work, a new set of conformational parameters for membrane spanning alpha helices was developed using the information from the topology of 70 membrane proteins. Based on these conformational parameters, a simple algorithm has been formulated to predict the transmembrane alpha helices in membrane proteins. A FORTRAN program has been developed which takes the amino acid sequence as input and gives the predicted transmembrane alpha-helices as output. The present method correctly identifies 295 transmembrane helical segments in 70 membrane proteins with only two overpredictions. Furthermore, this method predicts all 45 transmembrane helices in the photosynthetic reaction center, bacteriorhodopsin and cytochrome c oxidase to an 86% level of accuracy and so is better than all other methods published to date.
Gromiha
M M
MM
Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan.
D000465:Algorithms; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012984:Software
D045322:Photosynthetic Reaction Center Complex Proteins; D011506:Proteins; D001436:Bacteriorhodopsins; D003576:Electron Transport Complex IV