Titre de série :	Topics in Current Chemistry
Titre :	Vol.337 : Dynamics in enzyme catalysis
Type de document :	texte imprimé
Auteurs :	Judith Klinman, Éditeur scientifique ; Sharon Hammes- Schiffer, Éditeur scientifique
Editeur :	Berlin, Heidelberg : Springer
Année de publication :	2013
Collection :	Topics in Current Chemistry, ISSN 0340-1022 num. 337
Importance :	ix, 212 p.
Présentation :	ill. en noir et en coul.
Format :	24 cm
ISBN/ISSN/EAN :	978-3-642-38961-0
Langues :	Anglais (eng)
Note de contenu :	"* Relationship of femtosecond–picosecond dynamics to enzyme-catalyzed H-transfer * Protein conformational disorder and enzyme catalysis * A surprising role for conformational entropy in protein function * Conformational heterogeneity within the LID domain mediates substrate binding to escherichia coli adenylate kinase: Function follows fluctuations * Structured crowding and its effects on enzyme catalysis * Allosteric activation transitions in enzymes and biomolecular motors:Insights from atomistic and coarse-grained simulations * Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase * Protein dynamics and the enzymatic reaction coordinate."
Cote :	EXCLU (SdL)
Num_Inv :	3194

Topics in Current Chemistry. Vol.337 : Dynamics in enzyme catalysis [texte imprimé] / Judith Klinman, Éditeur scientifique ; Sharon Hammes- Schiffer, Éditeur scientifique . - Berlin, Heidelberg : Springer, 2013 . - ix, 212 p. : ill. en noir et en coul. ; 24 cm. - (Topics in Current Chemistry, ISSN 0340-1022; 337) .
ISBN : 978-3-642-38961-0
Langues : Anglais (eng)

Note de contenu :	"* Relationship of femtosecond–picosecond dynamics to enzyme-catalyzed H-transfer * Protein conformational disorder and enzyme catalysis * A surprising role for conformational entropy in protein function * Conformational heterogeneity within the LID domain mediates substrate binding to escherichia coli adenylate kinase: Function follows fluctuations * Structured crowding and its effects on enzyme catalysis * Allosteric activation transitions in enzymes and biomolecular motors:Insights from atomistic and coarse-grained simulations * Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase * Protein dynamics and the enzymatic reaction coordinate."
Cote :	EXCLU (SdL)
Num_Inv :	3194