Intrinsically disordered regions may lower the hydration free energy in proteins: a case study of nudix hydrolase in the bacterium Deinococcus radiodurans.

Awile, Omar; Krisko, Anita; Sbalzarini, Ivo F; Zagrovic, Bojan

Awile, Omar; Krisko, Anita; Sbalzarini, Ivo F; Zagrovic, Bojan.

Affiliation

Awile O; Mediterranean Institute for Life Sciences, Split, Croatia.

PLoS Comput Biol ; 6(7): e1000854, 2010 Jul 15.

Article in En | MEDLINE | ID: mdl-20657662

Subject(s)

Bacterial Proteins/chemistry; Deinococcus/enzymology; Molecular Dynamics Simulation; Pyrophosphatases/chemistry; Desiccation; Hydrophobic and Hydrophilic Interactions; Protein Conformation; Sequence Analysis, Protein; Surface Properties; Thermodynamics; Water/chemistry; Nudix Hydrolases

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pyrophosphatases / Bacterial Proteins / Deinococcus / Molecular Dynamics Simulation Language: En Journal: PLoS Comput Biol Journal subject: BIOLOGIA / INFORMATICA MEDICA Year: 2010 Type: Article Affiliation country: Croatia

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