Literature DB >> 14607089

Atom depth in protein structure and function.

Alessandro Pintar1, Oliviero Carugo, Sándor Pongor.   

Abstract

Atom depth, originally defined as the distance between a protein atom and the nearest water molecule surrounding a protein, is a simple but valuable geometrical descriptor of the protein interior. It can be easily computed from the 3D structure of a protein, thus complementing the information provided by the calculation of the solvent accessible surface area and buried surface area. Depth has been found to be correlated with several molecular, residue and atomic properties, such as average protein domain size, protein stability, free energy of formation of protein complexes, amino acid type hydrophobicity, residue conservation and hydrogen/deuterium amide proton exchange rates.

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Year:  2003        PMID: 14607089     DOI: 10.1016/j.tibs.2003.09.004

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  18 in total

1.  A stringent test for hydrophobicity scales: two proteins with 88% sequence identity but different structure and function.

Authors:  Alexander E Kister; James C Phillips
Journal:  Proc Natl Acad Sci U S A       Date:  2008-06-30       Impact factor: 11.205

2.  Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate.

Authors:  Brad Bennett; Paul Langan; Leighton Coates; Marat Mustyakimov; Benno Schoenborn; Elizabeth E Howell; Chris Dealwis
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-27       Impact factor: 11.205

3.  Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.

Authors:  Gabrielle Stetz; Gennady M Verkhivker
Journal:  PLoS One       Date:  2015-11-30       Impact factor: 3.240

4.  Shape and evolution of thermostable protein structure.

Authors:  Ryan G Coleman; Kim A Sharp
Journal:  Proteins       Date:  2010-02-01

5.  DEPTH: a web server to compute depth and predict small-molecule binding cavities in proteins.

Authors:  Kuan Pern Tan; Raghavan Varadarajan; M S Madhusudhan
Journal:  Nucleic Acids Res       Date:  2011-05-16       Impact factor: 16.971

6.  Prediction of functionally important residues in globular proteins from unusual central distances of amino acids.

Authors:  Marek Kochańczyk
Journal:  BMC Struct Biol       Date:  2011-09-18

7.  DBAC: a simple prediction method for protein binding hot spots based on burial levels and deeply buried atomic contacts.

Authors:  Zhenhua Li; Limsoon Wong; Jinyan Li
Journal:  BMC Syst Biol       Date:  2011-06-20

8.  Prodepth: predict residue depth by support vector regression approach from protein sequences only.

Authors:  Jiangning Song; Hao Tan; Khalid Mahmood; Ruby H P Law; Ashley M Buckle; Geoffrey I Webb; Tatsuya Akutsu; James C Whisstock
Journal:  PLoS One       Date:  2009-09-17       Impact factor: 3.240

9.  Characterization of non-trivial neighborhood fold constraints from protein sequences using generalized topohydrophobicity.

Authors:  Guillaume Fourty; Isabelle Callebaut; Jean-Paul Mornon
Journal:  Bioinform Biol Insights       Date:  2008-01-31

10.  Depth: a web server to compute depth, cavity sizes, detect potential small-molecule ligand-binding cavities and predict the pKa of ionizable residues in proteins.

Authors:  Kuan Pern Tan; Thanh Binh Nguyen; Siddharth Patel; Raghavan Varadarajan; M S Madhusudhan
Journal:  Nucleic Acids Res       Date:  2013-06-12       Impact factor: 16.971

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