Literature DB >> 19275897

The courtship of proteins: understanding the encounter complex.

Marcellus Ubbink1.   

Abstract

The formation of protein complexes involves an encounter complex, in which proteins show few specific interactions and assume many orientations. Recent kinetic and structural studies have shed light on this elusive state. It is generally dominated by electrostatic interactions, although hydrophobic interactions can play a role. During the encounter phase the proteins remain largely solvated. In extreme cases, the proteins only form an encounter complex, and in many other complexes, the encounter state constitutes a significant amount (5% or more), indicating that the energy difference between encounter and productive complexes is small. Thus, the encounter complex represents an essential part of protein complexes.

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Year:  2009        PMID: 19275897     DOI: 10.1016/j.febslet.2009.02.046

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


  60 in total

1.  A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data.

Authors:  Shivani Ahuja; Nicole Jahr; Sang-Choul Im; Subramanian Vivekanandan; Nataliya Popovych; Stéphanie V Le Clair; Rui Huang; Ronald Soong; Jiadi Xu; Kazutoshi Yamamoto; Ravi P Nanga; Angela Bridges; Lucy Waskell; Ayyalusamy Ramamoorthy
Journal:  J Biol Chem       Date:  2013-05-24       Impact factor: 5.157

2.  Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.

Authors:  Alexander N Volkov; Marcellus Ubbink; Nico A J van Nuland
Journal:  J Biomol NMR       Date:  2010-11-04       Impact factor: 2.835

3.  Synergic role of nucleophosmin three-helix bundle and a flanking unstructured tail in the interaction with G-quadruplex DNA.

Authors:  Alessandro Arcovito; Sara Chiarella; Stefano Della Longa; Adele Di Matteo; Carlo Lo Sterzo; Giovanni Luca Scaglione; Luca Federici
Journal:  J Biol Chem       Date:  2014-06-21       Impact factor: 5.157

Review 4.  smFRET studies of the 'encounter' complexes and subsequent intermediate states that regulate the selectivity of ligand binding.

Authors:  Colin D Kinz-Thompson; Ruben L Gonzalez
Journal:  FEBS Lett       Date:  2014-07-24       Impact factor: 4.124

Review 5.  Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.

Authors:  G Marius Clore
Journal:  Protein Sci       Date:  2011-02       Impact factor: 6.725

6.  Direct visualization reveals dynamics of a transient intermediate during protein assembly.

Authors:  Xin Zhang; Vinh Q Lam; Yun Mou; Tetsunari Kimura; Jaeyoon Chung; Sowmya Chandrasekar; Jay R Winkler; Stephen L Mayo; Shu-ou Shan
Journal:  Proc Natl Acad Sci U S A       Date:  2011-04-04       Impact factor: 11.205

7.  Heterogeneous and Highly Dynamic Interface in Plastocyanin-Cytochrome f Complex Revealed by Site-Specific 2D-IR Spectroscopy.

Authors:  Sashary Ramos; Amanda L Le Sueur; Rachel E Horness; Jonathan T Specker; Jessica A Collins; Katherine E Thibodeau; Megan C Thielges
Journal:  J Phys Chem B       Date:  2019-02-21       Impact factor: 2.991

8.  Identification of productive and futile encounters in an electron transfer protein complex.

Authors:  Witold Andrałojć; Yoshitaka Hiruma; Wei-Min Liu; Enrico Ravera; Masaki Nojiri; Giacomo Parigi; Claudio Luchinat; Marcellus Ubbink
Journal:  Proc Natl Acad Sci U S A       Date:  2017-02-21       Impact factor: 11.205

9.  Mechanistic details of a protein-protein association pathway revealed by paramagnetic relaxation enhancement titration measurements.

Authors:  Nicolas L Fawzi; Michaeleen Doucleff; Jeong-Yong Suh; G Marius Clore
Journal:  Proc Natl Acad Sci U S A       Date:  2010-01-07       Impact factor: 11.205

Review 10.  Hub promiscuity in protein-protein interaction networks.

Authors:  Ashwini Patil; Kengo Kinoshita; Haruki Nakamura
Journal:  Int J Mol Sci       Date:  2010-04-26       Impact factor: 5.923

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