Literature DB >> 8612074

Packing interactions in the apomyglobin folding intermediate.

M S Kay1, R L Baldwin.   

Abstract

The contribution of specific packing to the stability of the sperm whale apomyoglobin intermediate has been studied by urea denaturation monitored by circular dichroism and fluorescence. Mutations disrupting native packing sites within the subdomain formed by the A, G and H helices destabilize the intermediate, in contrast to the conclusion drawn from earlier studies of pH-induced unfolding. Based on these results, the intermediate is proposed to be stabilized by both partially formed native-like tertiary, and non-specific hydrophobic interactions forming a subdomain folding intermediate. The results help to explain how the intermediate acquires its structure and stability.

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Year:  1996        PMID： 8612074     DOI： 10.1038/nsb0596-439

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN： 1072-8368


  32 in total

1.  The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding.

Authors:  Y Luo; R L Baldwin
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

2.  The major transition state in folding need not involve the immobilization of side chains.

Authors:  R A Staniforth; J L Dean; Q Zhong; E Zerovnik; A R Clarke; J P Waltho
Journal:  Proc Natl Acad Sci U S A       Date:  2000-05-23       Impact factor: 11.205

3.  The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry.

Authors:  M Jamin; M Antalik; S N Loh; D W Bolen; R L Baldwin
Journal:  Protein Sci       Date:  2000-07       Impact factor: 6.725

4.  What causes hyperfluorescence: folding intermediates or conformationally flexible native states?

Authors:  John Ervin; Edgar Larios; Szabolcs Osváth; Klaus Schulten; Martin Gruebele
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

5.  Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness.

Authors:  Takanori Uzawa; Shuji Akiyama; Tetsunari Kimura; Satoshi Takahashi; Koichiro Ishimori; Isao Morishima; Tetsuro Fujisawa
Journal:  Proc Natl Acad Sci U S A       Date:  2004-01-07       Impact factor: 11.205

6.  Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region.

Authors:  Angela M Bertagna; Doug Barrick
Journal:  Proc Natl Acad Sci U S A       Date:  2004-08-16       Impact factor: 11.205

7.  Resolution of the effects induced by W → F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F.

Authors:  Giuseppe Infusini; Clara Iannuzzi; Silvia Vilasi; Leila Birolo; Daniela Pagnozzi; Piero Pucci; Gaetano Irace; Ivana Sirangelo
Journal:  Eur Biophys J       Date:  2012-06-22       Impact factor: 1.733

8.  Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate.

Authors:  M S Kay; C H Ramos; R L Baldwin
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-02       Impact factor: 11.205

9.  Differences in the folding transition state of ubiquitin indicated by phi and psi analyses.

Authors:  Tobin R Sosnick; Robin S Dothager; Bryan A Krantz
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-02       Impact factor: 11.205

10.  Three-state protein folding: experimental determination of free-energy profile.

Authors:  Ekaterina N Baryshnikova; Bogdan S Melnik; Alexei V Finkelstein; Gennady V Semisotnov; Valentina E Bychkova
Journal:  Protein Sci       Date:  2005-09-09       Impact factor: 6.725
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