Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F) [electronic resource]

By:

Liepinsh, E

Contributor(s):

Kitamura, M
Murakami, T
Nakaya, T
Otting, G

Producer: 19980115Description: 975-9 p. digitalISSN:

1072-8368

Subject(s):

Amino Acid Sequence
Bacterial Proteins -- chemistry
Binding Sites
Carrier Proteins -- chemistry
Chymotrypsin -- chemistry
Desulfovibrio vulgaris -- genetics
Evolution, Molecular
Flavoproteins
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure, Secondary
Sequence Homology, Amino Acid

Online resources:

Available from publisher's website

In: Nature structural biology vol. 4

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Publication Type: Letter; Research Support, Non-U.S. Gov't

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Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)

APA

Liepinsh E., Kitamura M., Murakami T., Nakaya T. & Otting G. (19980115). Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F). : Nature structural biology.

Chicago

Liepinsh E, Kitamura M, Murakami T, Nakaya T and Otting G. 19980115. Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F). : Nature structural biology.

Harvard

Liepinsh E., Kitamura M., Murakami T., Nakaya T. and Otting G. (19980115). Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F). : Nature structural biology.

MLA

Liepinsh E, Kitamura M, Murakami T, Nakaya T and Otting G. Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F). : Nature structural biology. 19980115.

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