A two-way structure
Article Abstract:
Structurally similar motor domains of myosin, kinesin and ncd encourage two-way movement along microtubules. The comparison of crystal structures of myosin, kinesin and ncd by aligning the P-loop shows a high degree of overlap of secondary structure elements between them. However, no such overlap is possible when they are compared to the other P-loop proteins. Despite similarities of energy transduction mechanisms, different techniques for the amplification of small structural changes are used in myosin and kinesin cycles.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Two heads are better than one
Article Abstract:
Two research studies conducted on single kinesin motors show that cooperative interactions between the two mechanochemical heads of the native protein influence the ability of the motors to move processively on microtubules. In vivo functions of kinesin and myosin are distinct, with the kinesin mechanochemical cycle being basically different from that of myosin. The two heads of the kinesin dimer interact and this interaction allows kinesin to remain attached to the microtubule.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Differences in the chemical reactivity of individual molecules of an enzyme
Article Abstract:
Examination of the reactivity of individual molecules of lactate dehydrogenase by fluorescence spectroscopy reveals the significant differences among the activity of individual electrophoretically pure enzyme molecules. This activity differences remain constant for a period of over two hours. Existence of various stable forms of the enzyme accounts for the differences in the chemical reactivity of individual enzyme molecule.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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