Study and prediction of secondary structure for membrane proteins.
In this paper we present a novel approach to membrane protein secondary structure prediction based on the statistical stepwise discriminant analysis method. A new aspect of our approach is the possibility to derive physical-chemical properties that may affect the formation of membrane protein secondary structure. The certain physical-chemical properties of protein chains can be used to clarify the formation of the secondary structure types under consideration. Another aspect of our approach is that the results of multiple sequence alignment, or the other kinds of sequence alignment, are not used in the frame of the method. Using our approach, we predicted the formation of three main secondary structure types (alpha-helix, beta-structure and coil) with high accuracy, that is Q(3) = 76%. Predicting the formation of alpha-helix and non-alpha-helix states we reached the accuracy which was measured as Q(2) = 86%. Also we have identified certain protein chain properties that affect the formation of membrane protein secondary structure. These protein properties include hydrophobic properties of amino acid residues, presence of Gly, Ala and Val amino acids, and the location of protein chain end.
Amirova
Svetlana R
SR
School of Computing and Mathematics, University of Keele, Staffordshire ST5 5BG, UK. s.amirova@epsam.keele.ac.uk
Milchevsky
Juri V
JV
Filatov
Ivan V
IV
Esipova
Natalia G
NG
Tumanyan
Vladimir G
VG
D000595:Amino Acid Sequence; D016002:Discriminant Analysis; D008565:Membrane Proteins / Q000737:chemistry* / Q000145:classification; D011336:Probability; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D012984:Software
D008565:Membrane Proteins