Literature DB >> 9377709

Transmuting alpha helices and beta sheets.

S Dalal1, S Balasubramanian, L Regan.   

Abstract

Protein architecture involves two main secondary structural classes: alpha helices and beta sheets. Some natural proteins alter their fold in response to changes in solution conditions or as a consequence of mutation. Here, we discuss recent attempts to induce such conformational changes by design: specifically, the motivation and success of efforts to change one protein fold into a different one in response to the 'Paracelsus Challenge'. The results of such efforts may provide a better understanding of the processes that underlie conformational plasticity in proteins.

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Year:  1997        PMID: 9377709     DOI: 10.1016/s1359-0278(97)00036-9

Source DB:  PubMed          Journal:  Fold Des        ISSN: 1359-0278


  13 in total

1.  New insight into the pH-dependent conformational changes in bovine beta-lactoglobulin from Raman optical activity.

Authors:  E W Blanch; L Hecht; L D Barron
Journal:  Protein Sci       Date:  1999-06       Impact factor: 6.725

2.  CKAAPs DB: a conserved key amino acid positions database.

Authors:  W W Li; B V Reddy; I N Shindyalov; P E Bourne
Journal:  Nucleic Acids Res       Date:  2001-01-01       Impact factor: 16.971

3.  Associative memory hamiltonians for structure prediction without homology: alpha-helical proteins.

Authors:  C Hardin; M P Eastwood; Z Luthey-Schulten; P G Wolynes
Journal:  Proc Natl Acad Sci U S A       Date:  2000-12-19       Impact factor: 11.205

4.  Understanding the sequence determinants of conformational switching using protein design.

Authors:  S Dalal; L Regan
Journal:  Protein Sci       Date:  2000-09       Impact factor: 6.725

5.  CKAAPs DB: a Conserved Key Amino Acid Positions DataBase.

Authors:  Wilfred W Li; Boojala V B Reddy; John G Tate; Ilya N Shindyalov; Philip E Bourne
Journal:  Nucleic Acids Res       Date:  2002-01-01       Impact factor: 16.971

6.  Solution structure and dynamics of bovine beta-lactoglobulin A.

Authors:  K Kuwata; M Hoshino; V Forge; S Era; C A Batt; Y Goto
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

7.  The design and characterization of two proteins with 88% sequence identity but different structure and function.

Authors:  Patrick A Alexander; Yanan He; Yihong Chen; John Orban; Philip N Bryan
Journal:  Proc Natl Acad Sci U S A       Date:  2007-07-03       Impact factor: 11.205

8.  NMR structures of two designed proteins with high sequence identity but different fold and function.

Authors:  Yanan He; Yihong Chen; Patrick Alexander; Philip N Bryan; John Orban
Journal:  Proc Natl Acad Sci U S A       Date:  2008-09-16       Impact factor: 11.205

9.  Proposed mechanism for stability of proteins to evolutionary mutations.

Authors:  E D Nelson; J N Onuchic
Journal:  Proc Natl Acad Sci U S A       Date:  1998-09-01       Impact factor: 11.205

10.  Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3.

Authors:  K Sakurai; M Oobatake; Y Goto
Journal:  Protein Sci       Date:  2001-11       Impact factor: 6.725

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