@ARTICLE{Surzhik2010206,
author={Surzhik, M.A. and Churkina, S.V. and Shmidt, A.E. and Shvetsov, A.V. and Kozhina, T.N. and Firsov, D.L. and Firsov, L.M. and Petukhov, M.G.},
title={The effect of point amino acid substitutions in an internal α-helix on thermostability of Aspergillus awamori X100 glucoamylase},
journal={Applied Biochemistry and Microbiology},
year={2010},
volume={46},
number={2},
pages={206-211},
doi={10.1134/S0003683810020134},
note={cited By 4},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-77952311178&doi=10.1134%2fS0003683810020134&partnerID=40&md5=32c7917eb15ba2847a518a070ad3cb0e},
affiliation={Konstantinov Petersburg Institute of Nuclear Physics, Russian Academy of Sciences, Gatchina Leningrad oblast, 188300, Russian Federation},
abstract={Conformational flexibility of α-helices in glucoamylase of the fungus Aspergillus awamori was studied by molecular dynamics methods. Several amino acid substitutions (G127A, P128A, I136L, G137A, and G139A) optimizing intrinsic interactions in one of the α-helices (D) within the hydrophobic core of this protein were constructed and studied. It was found that these point mutations had different effects on the glucoamylase thermal inactivation constant. Unlike amino acid substitution P128A and substitutions G137A and A246C, I136L and G139A displayed a pronounced additive thermostabilizing effect. © 2010 Pleiades Publishing, Ltd.},
funding_details={RNP.2.2.1.1.4663},
funding_details={Российский Фонд Фундаментальных Исследований (РФФИ)07 04 00785},
}

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Several amino acid substitutions (G127A, P128A, I136L, G137A, and G139A) optimizing intrinsic interactions in one of the α-helices (D) within the hydrophobic core of this protein were constructed and studied. It was found that these point mutations had different effects on the glucoamylase thermal inactivation constant. Unlike amino acid substitution P128A and substitutions G137A and A246C, I136L and G139A displayed a pronounced additive thermostabilizing effect. © 2010 Pleiades Publishing, Ltd.","funding_details":"Российский Фонд Фундаментальных Исследований (РФФИ)07 04 00785","bibtex":"@ARTICLE{Surzhik2010206,\r\nauthor={Surzhik, M.A. and Churkina, S.V. and Shmidt, A.E. and Shvetsov, A.V. and Kozhina, T.N. and Firsov, D.L. and Firsov, L.M. and Petukhov, M.G.},\r\ntitle={The effect of point amino acid substitutions in an internal α-helix on thermostability of Aspergillus awamori X100 glucoamylase},\r\njournal={Applied Biochemistry and Microbiology},\r\nyear={2010},\r\nvolume={46},\r\nnumber={2},\r\npages={206-211},\r\ndoi={10.1134/S0003683810020134},\r\nnote={cited By 4},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-77952311178&doi=10.1134%2fS0003683810020134&partnerID=40&md5=32c7917eb15ba2847a518a070ad3cb0e},\r\naffiliation={Konstantinov Petersburg Institute of Nuclear Physics, Russian Academy of Sciences, Gatchina Leningrad oblast, 188300, Russian Federation},\r\nabstract={Conformational flexibility of α-helices in glucoamylase of the fungus Aspergillus awamori was studied by molecular dynamics methods. Several amino acid substitutions (G127A, P128A, I136L, G137A, and G139A) optimizing intrinsic interactions in one of the α-helices (D) within the hydrophobic core of this protein were constructed and studied. It was found that these point mutations had different effects on the glucoamylase thermal inactivation constant. 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