Literature DB >> 1397302

Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin.

J A Carver1, J A Aquilina, R J Truscott, G B Ralston.   

Abstract

Two-dimensional 1H NMR spectroscopy of bovine eye lens alpha-crystallin and its isolated alpha A and alpha B subunits reveals that these aggregates have short and very flexible C-terminal extensions of eight (alpha A) and ten (alpha B) amino acids which adopt little preferred conformation in solution. Total alpha-crystallin forms a tighter aggregate than the isolated alpha A and alpha B subunit aggregates. Our results are consistent with a micelle model for alpha-crystallin quaternary structure. The presence of terminal extensions is a general feature of those crystallins, alpha and beta, which form aggregates.

Entities:  

Mesh：

Substances：

Year:  1992        PMID： 1397302     DOI： 10.1016/0014-5793(92)81386-z

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  39 in total

1.  Characterization of alpha-crystallin-plasma membrane binding.

Authors:  B A Cobb; J M Petrash
Journal:  J Biol Chem       Date:  2000-03-03       Impact factor: 5.157

2.  The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.

Authors:  R A Lindner; T M Treweek; J A Carver
Journal:  Biochem J       Date:  2001-02-15       Impact factor: 3.857

3.  Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity.

Authors:  P Fernando; J J Heikkila
Journal:  Cell Stress Chaperones       Date:  2000-04       Impact factor: 3.667

4.  Xenopus small heat shock proteins, Hsp30C and Hsp30D, maintain heat- and chemically denatured luciferase in a folding-competent state.

Authors:  Rashid Abdulle; Ashvin Mohindra; Pasan Fernando; John J Heikkila
Journal:  Cell Stress Chaperones       Date:  2002-01       Impact factor: 3.667

5.  Thermal stability of human alpha-crystallins sensed by amide hydrogen exchange.

Authors:  Azeem Hasan; Jiong Yu; David L Smith; Jean B Smith
Journal:  Protein Sci       Date:  2004-02       Impact factor: 6.725

6.  Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach.

Authors:  Nathalie Braun; Martin Zacharias; Jirka Peschek; Andreas Kastenmüller; Juan Zou; Marianne Hanzlik; Martin Haslbeck; Juri Rappsilber; Johannes Buchner; Sevil Weinkauf
Journal:  Proc Natl Acad Sci U S A       Date:  2011-12-05       Impact factor: 11.205

7.  The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.

Authors:  Andi Mainz; Jirka Peschek; Maria Stavropoulou; Katrin C Back; Benjamin Bardiaux; Sam Asami; Elke Prade; Carsten Peters; Sevil Weinkauf; Johannes Buchner; Bernd Reif
Journal:  Nat Struct Mol Biol       Date:  2015-10-12       Impact factor: 15.369

8.  Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation.

Authors:  Eri Ohto-Fujita; Yoshinobu Fujita; Yoriko Atomi
Journal:  Cell Stress Chaperones       Date:  2007       Impact factor: 3.667

9.  alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer.

Authors:  Stefan Jehle; Barth van Rossum; Joseph R Stout; Satoshi M Noguchi; Katja Falber; Kristina Rehbein; Hartmut Oschkinat; Rachel E Klevit; Ponni Rajagopal
Journal:  J Mol Biol       Date:  2008-11-14       Impact factor: 5.469

10.  Collisional activation of protein complexes: picking up the pieces.

Authors:  Justin L P Benesch
Journal:  J Am Soc Mass Spectrom       Date:  2008-11-27       Impact factor: 3.109
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.