Computer programs to identify and classify amphipathic alpha helical domains.

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Computer programs to identify and classify amphipathic alpha helical domains.

The amphipathic alpha helix is an often-encountered secondary structural motif in biologically active peptides and proteins. An amphipathic helix is defined as an alpha helix with opposing polar and nonpolar faces oriented along the long axis of the helix. In a recent review article we grouped amphipathic helixes into seven distinct classes (A, H, L, G, K, C, and M) based upon a detailed analys...

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apoB-100 has a pentapartite structure composed of three amphipathic alpha-helical domains alternating with two amphipathic beta-strand domains. Detection by the computer program LOCATE.

Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called Locate that searches amino acid sequences to identify potential amphipathic alpha-helixes and beta-strands by using sets of rules for helix and strand termination. A series of model chimeric prot...

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ApoB - 100 Has a Pentapartite Structure Composed of Three Amphipathic ar - Helical Domains Alternating With Two Amphipathic / 3 - Strand Domains Detection by the Computer Program

Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called LOCATE that searches amino acid sequences to identify potential amphipathic a-helixes and /3-strands by using sets of rules for helix and strand termination. A series of model chimeric protein te...

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1674 ApoB - 100 Has a Pentapartite Structure Composed of Three Amphipathic ar - Helical Domains Alternating With Two Amphipathic / 3 - Strand Domains Detection by the Computer Program

Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called LOCATE that searches amino acid sequences to identify potential amphipathic a-helixes and /3-strands by using sets of rules for helix and strand termination. A series of model chimeric protein te...

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ApoB-100 Has a Pentapartite Structure Composed of Three Amphipathic ar-Helical Domains Alternating With Two Amphipathic /3-Strand Domains

Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called LOCATE that searches amino acid sequences to identify potential amphipathic a-helixes and /3-strands by using sets of rules for helix and strand termination. A series of model chimeric protein te...

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ژورنال

عنوان ژورنال: Journal of Lipid Research

سال: 1992

ISSN: 0022-2275

DOI: 10.1016/s0022-2275(20)41549-4