α-Helix-to-random-coil transition of two-chain, coiled coils. Theory and experiments for thermal denaturation of α-tropomyosin at acidic pH

1983 ◽  
Vol 16 (3) ◽  
pp. 462-465 ◽  
Author(s):  
Marilyn Emerson Holtzer ◽  
Alfred Holtzer ◽  
Jeffrey Skolnick

1983 ◽  
Vol 16 (2) ◽  
pp. 173-180 ◽  
Author(s):  
Marilyn Emerson Holtzer ◽  
Alfred Holtzer ◽  
Jeffrey Skolnick


1984 ◽  
Vol 17 (11) ◽  
pp. 2445-2447 ◽  
Author(s):  
Lori L. Isom ◽  
Marilyn Emerson Holtzer ◽  
Alfred Holtzer




1985 ◽  
Vol 18 (6) ◽  
pp. 1083-1086 ◽  
Author(s):  
S. Yukioka ◽  
Ichiro Noda ◽  
Mitsuru Nagasawa ◽  
Marilyn Emerson Holtzer ◽  
Alfred Holtzer




2006 ◽  
Vol 17 (02) ◽  
pp. 235-246 ◽  
Author(s):  
GÖKHAN GÖKOĞLU ◽  
TARIK ÇELİK

In order to provide insights into the misfolding mechanism and the subsequent aggregate formation which cause what are known as the neurodegenerative polyglutamine diseases, we have simulated a 10-residue polyglutamine (poly-Q) chain in vacuum and in solvent by multicanonical method, which enabled us to study the system in a wide temperature range and discuss thermodynamic properties. It is understood that the system in vacuum shows two phase transitions, first of them occur at high temperature that is the well-known helix-coil transition and the second one is a solid-solid transition. However, the poly-Q chain in solvent is in a random coil state at higher temperatures, goes through a conformational change at T = 200 K and assumes predominantly a mixture of anti-parallel β-sheet and α-helix structures at low temperatures. One-residue glutamine dipeptide is also simulated and low-energy stable conformations are identified.



1982 ◽  
Vol 15 (3) ◽  
pp. 812-821 ◽  
Author(s):  
Jeffrey Skolnick ◽  
Alfred Holtzer




1982 ◽  
Vol 16 (4) ◽  
pp. 275-285 ◽  
Author(s):  
Hiromitsu Wakana ◽  
Takao Shigaki ◽  
Nobuhiko Saitô
Keyword(s):  


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