Homology modelling

inferences from tables of aligned sequences. Current Opinion in Structural Biology 1992, 2:242-247

Arthur Lesk, D. Ross Boswell

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The relationship between an individual amino acid sequence and its associated protein structure is deterministic, but has proved to be too subtle to understand in detail from studying the relationships between single amino acid sequences and structures. The patterns that appear in tables of aligned homologous sequences contain much more information, and study of them has led to success in several applications. These include: a priori predictions of secondary and tertiary structure, screening an amino acid sequence database for proteins that share a folding pattern with a probe molecule, and distinguishing between correct protein structures and erroneous ones.

Original languageEnglish (US)
Pages (from-to)242-247
Number of pages6
JournalCurrent Opinion in Structural Biology
Volume2
Issue number2
DOIs
StatePublished - Jan 1 1992

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Amino Acid Sequence
Protein Databases
Proteins
Sequence Homology

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

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Homology modelling : inferences from tables of aligned sequences. Current Opinion in Structural Biology 1992, 2:242-247. / Lesk, Arthur; Ross Boswell, D.

In: Current Opinion in Structural Biology, Vol. 2, No. 2, 01.01.1992, p. 242-247.

Research output: Contribution to journalArticle

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