Abstract
Transmembrane (TM) proteins fulfill many crucial cellular functions such as substrate transport, biogenesis and signalling, and make up a significant fraction of any given proteome. Estimates suggest that up to 30% of all human genes may encode α-helical TM proteins, while β-barrel TM proteins, which are found in the outer-membrane of gram-negative bacteria, mitochondria and chloroplast, are encoded by 2–3% of genes. However, relatively few high resolution TM protein structures are known, making it all the more important to extract as much structural information as possible from amino acid sequences. In this chapter, we review the existing methods for the identification, topology prediction and three-dimensional modelling of TM proteins, including a discussion of the recent advances in identifying residue-residue contacts from large multiple sequence alignments that have enabled impressive gains to be made in the field of TM protein structure prediction.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
