Influence of intermolecular interaction on kinetics of conformational transitions in poly-m-phenyleneisophthalamide

1985 ◽  
Vol 43 (2) ◽  
pp. 891-895
Author(s):  
P. M. Pakhomov ◽  
I. I. Novak ◽  
M. V. Shablygin ◽  
V. E. Korsukov
Keyword(s):  
Intermolecular Interaction ◽  
Conformational Transitions ◽  
Kinetics Of

Kinetics of thermally-induced conformational transitions in soybean protein films

Polymer ◽  
2010 ◽  
Vol 51 (11) ◽  
pp. 2410-2416 ◽  
Author(s):  
Kun Tian ◽  
David Porter ◽  
Jinrong Yao ◽  
Zhengzhong Shao ◽  
Xin Chen
Keyword(s):  
Soybean Protein ◽  
Conformational Transitions ◽  
Protein Films ◽  
Thermally Induced ◽  
Kinetics Of

scholarly journals Kinetics of Anesthetic-Induced Conformational Transitions in a Four-α-Helix Bundle Protein†

Biochemistry ◽  
2006 ◽  
Vol 45 (5) ◽  
pp. 1435-1441 ◽  
Author(s):  
Ken Solt ◽  
Jonas S. Johansson ◽  
Douglas E. Raines
Keyword(s):  
Conformational Transitions ◽  
Helix Bundle ◽  
Α Helix ◽  
Kinetics Of ◽  
Bundle Protein

Kinetics of deformation and intermolecular interaction in glassy polymers

1980 ◽  
Vol 22 (10) ◽  
pp. 2462-2471 ◽  
Author(s):  
V.A Bershtein ◽  
N.N Peschanskaya ◽  
V.A Stepanov
Keyword(s):  
Intermolecular Interaction ◽  
Glassy Polymers ◽  
Kinetics Of

scholarly journals Kinetics of Intermolecular Interaction during Protein Folding of Reduced Cytochrome c

2004 ◽  
Vol 87 (4) ◽  
pp. 2663-2675 ◽  
Author(s):  
Shinpei Nishida ◽  
Tomokazu Nada ◽  
Masahide Terazima
Keyword(s):  
Protein Folding ◽  
Cytochrome C ◽  
Intermolecular Interaction ◽  
Kinetics Of

Kinetics of conformational transitions in chain molecules

1980 ◽  
Vol 72 (10) ◽  
pp. 5489-5500 ◽  
Author(s):  
Jeffrey Skolnick ◽  
Eugene Helfand
Keyword(s):  
Conformational Transitions ◽  
Chain Molecules ◽  
Kinetics Of

The influence of D2O, perchlorate, and variation in temperature on the potential-dependent contractile function of frog skeletal muscle

1985 ◽  
Vol 63 (6) ◽  
pp. 693-703
Author(s):  
James G. Foulks ◽  
Lillian Morishita
Keyword(s):  
Skeletal Muscle ◽  
Contractile Function ◽  
Divalent Cations ◽  
Conformational Transitions ◽  
The Other ◽  
Frog Skeletal Muscle ◽  
Solvent Structure ◽  
Opposing Effects ◽  
Kinetics Of ◽  
Reduced Temperature

D2O and perchlorate manifest opposing effects on the contractile function of skeletal muscle (amplitude of twitches and maximum K contractures, potential dependence of contraction activation and inactivation), and when combined the influence of one may effectively antagonize that of the other. The ratio of perchlorate concentrations required to produce effects of equal intensity (e.g., twitch enhancement and restoration of maximum K contractures in media lacking divalent cations or containing a depressant concentration of a cationic amphipath) in H2O and D2O solutions was generally rather constant. These findings are compatible with the view that both agents can influence contractile function by virtue of their effects on solvent structure. In the absence of divalent cations, the effects of reduced temperature resemble those of D2O whereas the effects of increased temperature resemble those of the chaotropic anion. However, in other media, variation in temperature was found to result in additional nonsolvent effects so that low temperature could oppose rather than enhance the effects of D2O. These observations are discussed in terms of a model which postulates a role for solvent influences on the kinetics of two separate potential-dependent conformational transitions of membrane proteins which mediate the activation and inactivation of contraction in skeletal muscle.

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