Linked Life Data

131577

Source:http://linkedlifedata.com/resource/pubmed/id/131577

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1976-8-2
pubmed:abstractText
If we select for consideration any reaction M1 in equilibrium M2 in the myosin-ATPase cycle, the question arises as to the relations between the rate constants for (1) M1 equilibrium M2, (2) AM1 in equilibrium AM2 (A = actin), (3) A + M1 in equilibrium AM1, and (4) A + M2 equilibrium AM2, with actin and myosin either (a) in solution or (b) in the myofilament structure. It is shown here, by means of examples, that a single so-called potential of mean force, W, and structural free energy, Am, suffice to determine the reaction free energy surfaces for all of these transitions (W for the solution case, W + Am for the structured case). In fact, Am is the same for all reactions in the myosin-ATPase cycle. Of course, though indispensable as the starting point and adequate for qualitative understanding, the reaction free energy surface does not provide (without additional theory) the actual values of the rate constants or of the corresponding basic free energy changes in the myosin states involved. These rate constants and free energies are discussed, in a preliminary way, in two other papers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1629-35
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Reaction free energy surfaces in myosin-actin-ATP systems.
pubmed:publicationType
Journal Article