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268 related items for PubMed ID: 10737931

  • 1. Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein.
    Schuler B, Fürst F, Osterroth F, Steinbacher S, Huber R, Seckler R.
    Proteins; 2000 Apr 01; 39(1):89-101. PubMed ID: 10737931
    [Abstract] [Full Text] [Related]

  • 2. Mutations that stabilize folding intermediates of phage P22 tailspike protein: folding in vivo and in vitro, stability, and structural context.
    Beissinger M, Lee SC, Steinbacher S, Reinemer P, Huber R, Yu MH, Seckler R.
    J Mol Biol; 1995 May 26; 249(1):185-94. PubMed ID: 7776371
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  • 3. P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain.
    Schuler B, Seckler R.
    J Mol Biol; 1998 Aug 14; 281(2):227-34. PubMed ID: 9698543
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  • 4. Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.
    Miller S, Schuler B, Seckler R.
    Protein Sci; 1998 Oct 14; 7(10):2223-32. PubMed ID: 9792111
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  • 5. Side-chain specificity at three temperature-sensitive folding mutation sites of P22 tailspike protein.
    Lee SC, Yu MH.
    Biochem Biophys Res Commun; 1997 Apr 28; 233(3):857-62. PubMed ID: 9168948
    [Abstract] [Full Text] [Related]

  • 6. The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization.
    Kreisberg JF, Betts SD, Haase-Pettingell C, King J.
    Protein Sci; 2002 Apr 28; 11(4):820-30. PubMed ID: 11910025
    [Abstract] [Full Text] [Related]

  • 7. Mechanism of phage P22 tailspike protein folding mutations.
    Danner M, Seckler R.
    Protein Sci; 1993 Nov 28; 2(11):1869-81. PubMed ID: 8268798
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  • 8. Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity.
    Baxa U, Steinbacher S, Weintraub A, Huber R, Seckler R.
    J Mol Biol; 1999 Oct 29; 293(3):693-701. PubMed ID: 10543960
    [Abstract] [Full Text] [Related]

  • 9. Characterization of the protrimer intermediate in the folding pathway of the interdigitated beta-helix tailspike protein.
    Benton CB, King J, Clark PL.
    Biochemistry; 2002 Apr 23; 41(16):5093-103. PubMed ID: 11955057
    [Abstract] [Full Text] [Related]

  • 10. Invivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes.
    Reich L, Becker M, Seckler R, Weikl TR.
    Biophys Chem; 2009 May 23; 141(2-3):186-92. PubMed ID: 19254821
    [Abstract] [Full Text] [Related]

  • 11. Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase.
    Haase-Pettingell C, King J.
    J Mol Biol; 1997 Mar 21; 267(1):88-102. PubMed ID: 9096209
    [Abstract] [Full Text] [Related]

  • 12. A reversibly unfolding fragment of P22 tailspike protein with native structure: the isolated beta-helix domain.
    Miller S, Schuler B, Seckler R.
    Biochemistry; 1998 Jun 23; 37(25):9160-8. PubMed ID: 9636063
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  • 14. Stalled folding mutants in the triple beta-helix domain of the phage P22 tailspike adhesin.
    Weigele PR, Haase-Pettingell C, Campbell PG, Gossard DC, King J.
    J Mol Biol; 2005 Dec 16; 354(5):1103-17. PubMed ID: 16289113
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