Literature DB >> 3185721

A peptide model of a protein folding intermediate.

T G Oas1, P S Kim.   

Abstract

It is difficult to determine the structures of protein folding intermediates because folding is a highly cooperative process. A disulphide-bonded peptide pair, designed to mimic the first crucial intermediate in the folding of bovine pancreatic trypsin inhibitor, contains secondary and tertiary structure similar to that found in the native protein. Peptide models like this circumvent the problem of cooperativity and permit characterization of structures of folding intermediates.

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Year:  1988        PMID: 3185721     DOI: 10.1038/336042a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  37 in total

1.  A physical basis for protein secondary structure.

Authors:  R Srinivasan; G D Rose
Journal:  Proc Natl Acad Sci U S A       Date:  1999-12-07       Impact factor: 11.205

2.  Folding of an isolated ribonuclease H core fragment.

Authors:  A K Chamberlain; K F Fischer; D Reardon; T M Handel; A S Marqusee
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

3.  Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.

Authors:  J A Zitzewitz; P J Gualfetti; I A Perkons; S A Wasta; C R Matthews
Journal:  Protein Sci       Date:  1999-06       Impact factor: 6.725

4.  Lysozyme among the Lilliputians.

Authors:  G D Rose
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-18       Impact factor: 11.205

5.  A cavity-forming mutation in insulin induces segmental unfolding of a surrounding alpha-helix.

Authors:  Bin Xu; Qing-Xin Hua; Satoe H Nakagawa; Wenhua Jia; Ying-Chi Chu; Panayotis G Katsoyannis; Michael A Weiss
Journal:  Protein Sci       Date:  2002-01       Impact factor: 6.725

6.  Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR.

Authors:  D D Ojennus; M R Fleissner; D S Wuttke
Journal:  Protein Sci       Date:  2001-11       Impact factor: 6.725

7.  Bypassing the kinetic trap of serpin protein folding by loop extension.

Authors:  H Im; H Y Ahn; M H Yu
Journal:  Protein Sci       Date:  2000-08       Impact factor: 6.725

8.  Comparison of solution structures of mutant bovine pancreatic trypsin inhibitor proteins using two-dimensional nuclear magnetic resonance.

Authors:  M R Hurle; C D Eads; D A Pearlman; G L Seibel; J Thomason; P A Kosen; P Kollman; S Anderson; I D Kuntz
Journal:  Protein Sci       Date:  1992-01       Impact factor: 6.725

9.  The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.

Authors:  C P van Mierlo; N J Darby; T E Creighton
Journal:  Proc Natl Acad Sci U S A       Date:  1992-08-01       Impact factor: 11.205

10.  Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor.

Authors:  J S Weissman; P S Kim
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-15       Impact factor: 11.205

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