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Search: WFRF:(Metzger S.) > (2010-2014) > Predicting Structur...

  • Metzger, Jennifer (author)

Predicting Structural and Functional Properties of Membrane Proteins from Protein Sequence

  • Article/chapterEnglish2011

Publisher, publication year, extent ...

  • Amsterdam :Elsevier Science BV,2011
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:su-94443
  • https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-94443URI
  • https://doi.org/10.1016/B978-0-444-53835-2.00002-XDOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:kap swepub-publicationtype

Notes

  • Integral transmembrane (TM) proteins are essential constituents of biological membranes where they fulfill a variety of important cellular functions. Because of difficulties with determining their structures by experimental techniques, comparably few 3D structures of membrane proteins are known so far. Therefore, computational methods trained on the available structures using only the protein sequence as input have become important tools in this field. In this chapter, we give a short introduction to the topic and then summarize recent bioinformatics tools for the prediction of structural as well as functional properties of alpha-helical and beta-barrel TM proteins. We present methods that allow predicting the locations of alpha-helical and beta-strand TM segments, to determine the exposure status of residues in the TM region to the surrounding lipids, and that allow functional annotations from the protein sequence.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Schaadt, Nadine S. (author)
  • Hayat, SikanderStockholms universitet,Institutionen för biokemi och biofysik (author)
  • Helms, Volkhard (author)
  • Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)

Related titles

  • In:Annual Reports in Computational ChemistryAmsterdam : Elsevier Science BV, s. 39-649780444543028

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