Article ; Online: De novo membrane protein structure prediction.
Methods in molecular biology (Clifton, N.J.)
2015 Volume 1215, Page(s) 331–350
Abstract: Recent advances in identifying residue-residue contacts from large multiple sequence alignments have enabled impressive gains to be made in the field of protein structure prediction. In this chapter, we discuss these advances and provide a step-by-step ... ...
Abstract | Recent advances in identifying residue-residue contacts from large multiple sequence alignments have enabled impressive gains to be made in the field of protein structure prediction. In this chapter, we discuss these advances and provide a step-by-step guide to applying the latest tools to the de novo modelling of alpha-helical transmembrane proteins. As a practical example, we demonstrate the process of building an accurate 3D model of a G protein-coupled receptor, correctly orientated in the membrane, using only its primary protein sequence. |
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MeSH term(s) | Amino Acid Sequence ; Animals ; Cattle ; Computational Biology/methods ; Membrane Proteins/chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; Rhodopsin/chemistry ; Temperature |
Chemical Substances | Membrane Proteins ; Rhodopsin (9009-81-8) |
Language | English |
Publishing date | 2015 |
Publishing country | United States |
Document type | Journal Article |
ISSN | 1940-6029 |
ISSN (online) | 1940-6029 |
DOI | 10.1007/978-1-4939-1465-4_15 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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