Skeletal muscle myosin light chain kinase. A refined structural model.
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Skeletal muscle myosin light chain kinase. A refined structural model. / Mayr, Georg W.; Heilmeyer, L M.
in: FEBS LETT, Jahrgang 157, Nr. 2, 2, 1983, S. 225-231.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Skeletal muscle myosin light chain kinase. A refined structural model.
AU - Mayr, Georg W.
AU - Heilmeyer, L M
PY - 1983
Y1 - 1983
N2 - A hydrodynamic, enzymatic and CD spectroscopic study of skeletal muscle myosin light chain kinase, three proteolytic fragments and corresponding complexes with calmodulin was performed. A refined shape model was built for the enzyme. It was shown that a head-and-tail structure is formed from two major fragments which are aligned end-to-end. The one fragment (Mr 36000) is compact, of high alpha-helix content and contains the catalytic center with the light chain and the calmodulin binding domains. The other fragment (Mr 33000) with unknown function is asymmetric (a/b greater than 10), of low alpha-helix and of unusually high proline content.
AB - A hydrodynamic, enzymatic and CD spectroscopic study of skeletal muscle myosin light chain kinase, three proteolytic fragments and corresponding complexes with calmodulin was performed. A refined shape model was built for the enzyme. It was shown that a head-and-tail structure is formed from two major fragments which are aligned end-to-end. The one fragment (Mr 36000) is compact, of high alpha-helix content and contains the catalytic center with the light chain and the calmodulin binding domains. The other fragment (Mr 33000) with unknown function is asymmetric (a/b greater than 10), of low alpha-helix and of unusually high proline content.
M3 - SCORING: Zeitschriftenaufsatz
VL - 157
SP - 225
EP - 231
JO - FEBS LETT
JF - FEBS LETT
SN - 0014-5793
IS - 2
M1 - 2
ER -
