Literature DB >> 34181188

A Minireview on Temperature Dependent Protein Conformational Sampling.

Ming Dong1.   

Abstract

In this minireview we discuss the role of the more subtle conformational change-protein conformational sampling and connect it to the classic relationship of protein structure and function. The theory of pre-existing functional states of protein are discussed in context of alternate protein conformational sampling. Last, we discuss how temperature, ligand binding and mutations affect the protein conformational sampling mode which is linked to the protein function regulation. The review includes several protein systems that showed temperature dependent protein conformational sampling. We also specifically included two enzyme systems, thermophilic alcohol dehydrogenase (ht-ADH) and thermolysin which we previously studied when discussing temperature dependent protein conformational sampling.
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Biphasic transition; Protein conformational sampling; Protein structure and function

Mesh:

Substances:

Year:  2021        PMID: 34181188     DOI: 10.1007/s10930-021-10012-x

Source DB:  PubMed          Journal:  Protein J        ISSN: 1572-3887            Impact factor:   2.371


  46 in total

1.  The effects of modifying the surface charge on the catalytic activity of a thermolysin-like protease.

Authors:  Arno de Kreij; Bertus van den Burg; Gerard Venema; Gert Vriend; Vincent G H Eijsink; Jens E Nielsen
Journal:  J Biol Chem       Date:  2002-02-21       Impact factor: 5.157

2.  Enzyme dynamics during catalysis.

Authors:  Elan Zohar Eisenmesser; Daryl A Bosco; Mikael Akke; Dorothee Kern
Journal:  Science       Date:  2002-02-22       Impact factor: 47.728

3.  Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K.

Authors:  R F Tilton; J C Dewan; G A Petsko
Journal:  Biochemistry       Date:  1992-03-10       Impact factor: 3.162

4.  Conformational dynamics of free and catalytically active thermolysin are indistinguishable by hydrogen/deuterium exchange mass spectrometry.

Authors:  Yu-Hong Liu; Lars Konermann
Journal:  Biochemistry       Date:  2008-05-22       Impact factor: 3.162

5.  Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.

Authors:  Jennifer M Axe; Kathleen F O'Rourke; Nicole E Kerstetter; Eric M Yezdimer; Yan M Chan; Alexander Chasin; David D Boehr
Journal:  Protein Sci       Date:  2014-12-11       Impact factor: 6.725

6.  Amino acid networks in a (β/α)₈ barrel enzyme change during catalytic turnover.

Authors:  Jennifer M Axe; Eric M Yezdimer; Kathleen F O'Rourke; Nicole E Kerstetter; Wanli You; Chia-en A Chang; David D Boehr
Journal:  J Am Chem Soc       Date:  2014-05-02       Impact factor: 15.419

7.  Dynamical network of residue-residue contacts reveals coupled allosteric effects in recognition, catalysis, and mutation.

Authors:  Urmi Doshi; Michael J Holliday; Elan Z Eisenmesser; Donald Hamelberg
Journal:  Proc Natl Acad Sci U S A       Date:  2016-04-11       Impact factor: 11.205

Review 8.  The role of dynamic conformational ensembles in biomolecular recognition.

Authors:  David D Boehr; Ruth Nussinov; Peter E Wright
Journal:  Nat Chem Biol       Date:  2009-11       Impact factor: 15.040

9.  Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.

Authors:  P Závodszky; J Kardos; G A Petsko
Journal:  Proc Natl Acad Sci U S A       Date:  1998-06-23       Impact factor: 11.205

10.  Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.

Authors:  Corey W Meadows; Ryan Ou; Judith P Klinman
Journal:  J Phys Chem B       Date:  2014-06-03       Impact factor: 2.991

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