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Using Sequence Information to Identify Motifs

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Molecular Life Sciences
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Synopsis

Identifying potential functions for an unknown protein sequence has become easier due to the proliferation of powerful algorithms to compare the sequence to large databases of consensus domains and motifs. Understanding the use and the potential dangers of such algorithms can greatly speed any work with new and novel sequences. The most important thing to remember is that such programs can only create a hypothesis about the shape or function of a sequence, not prove any functions. Such programs are the first step in any study of a new protein, not the last.

Introduction

The flow of biological information from DNA to RNA to protein necessarily requires that the final shape of the protein is encoded into the DNA. This essential fact of biology is the basis for the field of bioinformatics. Bioinformatics greatly expands the knowledge of researchers about the potential functions of a given gene by simply examining the nucleotide or encoded-protein sequence. Another essential fact...

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References

  • Bagos PG, Liakopoulos TD, Spyropoulos IC, Hamodrakas SJ (2004) PRED-TMBB: a web server for predicting the topology of beta-barrel outer membrane proteins. Nucleic Acids Res 32(Webserver Issue):W400–W404

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Emanuelsson O, Brunak S, von Heijne G, Nielsen H (2007) Locating proteins in the cell using TargetP, SignalP, and related tools. Nat Protoc 2:953–971

    Article  CAS  PubMed  Google Scholar 

  • Krogh A, Larsson B, von Heijne G, Sonnhammer ELL (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305:567–580

    Article  CAS  PubMed  Google Scholar 

  • Pei J, Grishin NV (2001) GGDEF domain is homologous to adenylyl cyclase. Proteins 42:210–216

    Article  CAS  PubMed  Google Scholar 

  • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785–786

    Article  CAS  PubMed  Google Scholar 

  • Punta M, Coggill PC, Eberhardt RY, Mistry J, Tate J, Boursnell C, Pang N, Forslund K, Ceric G, Clements J, Heger A, Holm L, Sonnhammer ELL, Eddy SR, Bateman A, Finn RD (2012) The Pfam protein families database. Nucleic Acids Res 40(Database Issue):D290–D301

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Schwarz F, Aebi M (2011) Mechanisms and principles of N-linked protein glycosylation. Curr Opin Struct Biol 21:576–582

    Article  CAS  PubMed  Google Scholar 

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Correspondence to Anton Sanderfoot .

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© 2014 Springer Science+Business Media New York

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Cooper, S., Sanderfoot, A. (2014). Using Sequence Information to Identify Motifs. In: Bell, E. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6436-5_5-3

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  • DOI: https://doi.org/10.1007/978-1-4614-6436-5_5-3

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  • Publisher Name: Springer, New York, NY

  • Online ISBN: 978-1-4614-6436-5

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