Homology modelling and molecular dynamics simulations: comparative studies of human aquaporin-1.

Journal article

The structures of the mammalian water transport protein Aqp1 and of its bacterial homologue GlpF enables us to test whether homology models can be used to explore relationships between structure, dynamics and function in mammalian transport proteins. Molecular dynamics simulations (totalling almost 40 ns) were performed starting from: the X-ray structure of Aqp1; a homology model of Aqp1 based on the GlpF structure; and intermediate resolution structures of Aqp1 derived from electron microsco...

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Authors: Law, R; Sansom, MS

• Publication status: Published
• Journal: European biophysics journal : EBJ
• Volume: 33
• Issue: 6
• Pages: 477-489
• Publication date: 2004-10-01
• DOI: 10.1007/s00249-004-0398-z
• EISSN: 1432-1017
• ISSN: 0175-7571
• Language: English
• Keywords: Models, Chemical; Humans; Models, Molecular; Porosity; Structure-Activity Relationship; Sequence Homology, Amino Acid; Motion; Aquaporins; Water; Aquaporin 1; Kinetics; Protein Structure, Secondary; Protein Conformation; Blood Group Antigens