Literature DB >> 12496122

Labeling proteins via hole burning of their aromatic amino acids: pressure tuning spectroscopy of BPTI.

Markus Stübner1, Christoph Hecht, Josef Friedrich.   

Abstract

We demonstrate hole burning on a protein by using an intrinsic aromatic amino acid as a probe. The protein is bovine pancreatic trypsin inhibitor (BPTI), the labeled amino acid is tyrosine. Only one of the four tyrosines could be burned. As an application we present pressure tuning experiments from which the local compressibility around the burned tyrosine probe is determined.

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Year:  2002        PMID： 12496122      PMCID： PMC1302430          DOI： 10.1016/S0006-3495(02)75355-1

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


  13 in total

1.  Molecular dynamics simulation shows large volume fluctuations of proteins.

Authors:  F Tama; O Miyashita; A Kitao; N Go
Journal:  Eur Biophys J       Date:  2000       Impact factor: 1.733

2.  Spectral hole burning and selection of conformational substates in chromoproteins.

Authors:  J Friedrich; J Gafert; J Zollfrank; J Vanderkooi; J Fidy
Journal:  Proc Natl Acad Sci U S A       Date:  1994-02-01       Impact factor: 11.205

3.  A photoinduced persistent structural transformation of the special pair of a bacterial reaction center.

Authors:  N R Reddy; S V Kolaczkowski; G J Small
Journal:  Science       Date:  1993-04-02       Impact factor: 47.728

4.  Harmonic and anharmonic aspects in the dynamics of BPTI: a normal mode analysis and principal component analysis.

Authors:  S Hayward; A Kitao; N Go
Journal:  Protein Sci       Date:  1994-06       Impact factor: 6.725

Review 5.  Proteins in electric fields and pressure fields: experimental results.

Authors:  J Fidy; E Balog; M Köhler
Journal:  Biochim Biophys Acta       Date:  1998-08-18

Review 6.  Proteins in electric fields and pressure fields: basic aspects.

Authors:  M Köhler; J Friedrich; J Fidy
Journal:  Biochim Biophys Acta       Date:  1998-08-18

7.  Compressibility-structure relationship of globular proteins.

Authors:  K Gekko; Y Hasegawa
Journal:  Biochemistry       Date:  1986-10-21       Impact factor: 3.162

8.  Stark-effect experiments on photochemical holes in chromoproteins: protoporphyrin IX-substituted myoglobin.

Authors:  J Gafert; J Friedrich; F Parak
Journal:  Proc Natl Acad Sci U S A       Date:  1995-03-14       Impact factor: 11.205

9.  Adiabatic compressibility of globular proteins.

Authors:  B Gavish; E Gratton; C J Hardy
Journal:  Proc Natl Acad Sci U S A       Date:  1983-02       Impact factor: 11.205

10.  Structure of bovine pancreatic trypsin inhibitor at 125 K definition of carboxyl-terminal residues Gly57 and Ala58.

Authors:  S Parkin; B Rupp; H Hope
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1996-01-01
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  4 in total

1.  Molecular probes: what is the range of their interaction with the environment?

Authors:  H Lesch; J Schlichter; J Friedrich; J M Vanderkooi
Journal:  Biophys J       Date:  2004-01       Impact factor: 4.033

2.  Local compressibilities of proteins: comparison of optical experiments and simulations for horse heart cytochrome-c.

Authors:  Christina Scharnagl; Maria Reif; Josef Friedrich
Journal:  Biophys J       Date:  2005-04-15       Impact factor: 4.033

3.  Pigment spectra and intermolecular interaction potentials in glasses and proteins.

Authors:  I Renge; R van Grondelle; J P Dekker
Journal:  Biophys J       Date:  2007-06-08       Impact factor: 4.033

4.  Dynamic fluctuation of proteins watched in real time.

Authors:  Pál Ormos
Journal:  HFSP J       Date:  2008-10-16
  4 in total

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