Literature DB >> 11742109

Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements.

H P Kresse1, M Czubayko, G Nyakatura, G Vriend, C Sander, H Bloecker.   

Abstract

We converted the small homodimeric four-helix bundle repressor of primer protein (Rop) into a monomeric four-helix bundle by introduction of connecting loops. Both left- and right-handed four-helix bundles were produced. The left-handed bundles were more stable and were used to introduce biologically interesting peptides in one of the loops.

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Year:  2001        PMID: 11742109     DOI: 10.1093/protein/14.11.897

Source DB:  PubMed          Journal:  Protein Eng        ISSN: 0269-2139


  3 in total

1.  An unusual hydrophobic core confers extreme flexibility to HEAT repeat proteins.

Authors:  Christian Kappel; Ulrich Zachariae; Nicole Dölker; Helmut Grubmüller
Journal:  Biophys J       Date:  2010-09-08       Impact factor: 4.033

2.  Synthetic approach to stop-codon scanning mutagenesis.

Authors:  Lihua Nie; Jason J Lavinder; Mohosin Sarkar; Kimberly Stephany; Thomas J Magliery
Journal:  J Am Chem Soc       Date:  2011-03-31       Impact factor: 15.419

3.  A comprehensive analysis of non-sequential alignments between all protein structures.

Authors:  Alexej Abyzov; Valentin A Ilyin
Journal:  BMC Struct Biol       Date:  2007-11-16
  3 in total

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