Molecular dynamic study of subtilisin Carlsberg in aqueous and nonaqueous solvents
2008; Taylor & Francis; Volume: 35; Issue: 3 Linguagem: Inglês
10.1080/08927020802415670
ISSN1029-0435
AutoresAnthony Cruz, Eunice Ramírez, Alberto Santana, Gabriel Barletta, Gustavo E. López,
Tópico(s)Protein Interaction Studies and Fluorescence Analysis
ResumoAbstract Using molecular dynamics simulations, we have obtained an important insight into the structural and dynamical changes exerted by a nonaqueous solvent on the serine protease subtilisin Carlsberg. Our findings show that the structural properties of the subtilisin–acetonitrile (MeCN) system were sensitive to the amount of water present at the protein surface. A decrease or lack of water promoted the enzyme–MeCN interaction, which increased structural changes of the enzyme primarily at the surface loops. This effect caused variations on the secondary and tertiary structure of the protein and induced the opening of a pathway for the solvent to the protein core. Also, disturbance of the oxyanion hole was observed due to changes in the orientation in the Asn-155 side chain. The disruption of the oxyanion hole and the changes of the tertiary structure should affect the optimal activity of the enzyme. Keywords: enzyme catalysisessential watersenzyme stability Acknowledgements The authors acknowledge the High Performance Computing Facility of the University of Puerto Rico. G.L.B. acknowledges support of the NIH/SCORE (Grant No. S06 GM08102) and NIH/INBRE (Grant No. P20 RR-016470) programmes. G.E.L. acknowledges support of the NIH/SCORE (Grant No. 5S06GM08103-35) programme and NIH/INBRE (Grant No. P20 RR-016470). Notes 1. ancruz@uprm.edu 2. asantana@uprm.edu 3. gl_barletta@webmail.uprh.edu 4. glopez@uprm.edu Additional informationNotes on contributorsAnthony Cruz 1. 1. ancruz@uprm.edu Alberto Santana 2. 2. asantana@uprm.edu Gabriel Barletta 3. 3. gl_barletta@webmail.uprh.edu Gustavo E. López 4. 4. glopez@uprm.edu
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