Literature DB >> 16402896

Amino acid propensities revisited.

Orlando E Acevedo1, Leonardo R Lareo.   

Abstract

Statistical analysis of amino acid patterns in approximately 160,000 alpha-helices in experimentally determined structures revealed di-, tri-, and tetrapeptides, whose frequencies deviate most from the statistical model. Importantly, some sequences were never found in alpha- helices. This fact was detected initially with tripeptides, where nearly 1% of the possible sequences were never seen in the helical segments. For tetrapeptides, this effect is very strong and significant; almost 43% of the possible sequences never appear in alpha-helices. It is possible that there are some steric and energetic restrictions that do not allow these tetrameric amino acid sequences to form alpha-helical structure.

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Year:  2005        PMID: 16402896     DOI: 10.1089/omi.2005.9.391

Source DB:  PubMed          Journal:  OMICS        ISSN: 1536-2310


  2 in total

1.  Propensities of Some Amino Acid Pairings in α-Helices Vary with Length.

Authors:  Cevdet Nacar
Journal:  Protein J       Date:  2022-09-28       Impact factor: 4.000

2.  Context-independent, temperature-dependent helical propensities for amino acid residues.

Authors:  Robert J Moreau; Christian R Schubert; Khaled A Nasr; Marianna Török; Justin S Miller; Robert J Kennedy; Daniel S Kemp
Journal:  J Am Chem Soc       Date:  2009-09-16       Impact factor: 15.419

  2 in total

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