Review: Protein function at thermal extremes: balancing stability and flexibility

QTL mapping of temperature sensitivity reveals candidate genes for thermal adaptation and growth morphology in the plant pathogenic fungus Zymoseptoria tritici

“…For example, nonsynonymous substitutions can generate protein isoforms that differ for thermal stability and/or optimized function at different temperatures (Schoville et al, 2012). In a population, genetic diversity for thermal adaptation can be maintained by antagonistic pleiotropy (genetic trade-offs), in which an allele that has optimal function at one temperature exhibits maladaptation at a different temperature (Fields, 2001). A better understanding of the genetic basis of thermal adaptation is likely to provide insight into the ability of species to adapt to global climate change (Austin, 2007).…”

Comparative thermal unfolding study of psychrophilic and mesophilic subtilisin-like serine proteases by molecular dynamics simulations

“…It has been postulated that the increased molecular flexibility at low temperatures is achieved through weakening the intramolecular noncovalent interactions that stabilize the native protein 3D structure, which is usually accompanied by a reduction in the thermostability of the psychrophilic enzymes (D'Amico, Marx, Fields, 2001;Georlette et al, 2003Georlette et al, , 2004. However, comparative studies of different thermally adapted enzymes have suggested that the optimization of catalytic activity in psychrophilic enzymes at low temperatures is not necessarily ascribed to an overall increase in structural flexibility, but it is most likely the result of improved flexibility in localized regions that may influence the mobility of the functionally relevant regions (D'Amico et al, 2003;Fields, 2001;Georlette et al, 2004;Papaleo, Riccardi, Villa, Fantucci, & De Gioia, 2006;Papaleo, Tiberti, Invernizzi, Pasi, & Ranzani, 2011;Siddiqui & Cavicchioli, 2006;. Consequently, the question of whether the often observed decrease in thermostability of the psychrophilic enzymes is caused by an increase in global or local flexibility needs to be further explored.…”

Purification and Characterization of Lactate Dehydrogenase A4Isozyme in Mandrin Fish (Siniperca scherzeri)

“…또한 종양세포를 유지함에 있어 산소 의존성이 낮은 대사과정을 필요로 하는 암세포의 경우 LDH A4 동위효소가 피루브산을 젖산으로 원활히 환원시켜 효과적인 혐기적 해당과정을 수행한다 [13,25]. LDH A4 동위 효소는 일반적으로 B4 동위효소보다 열에 불안정하고 [42,43], 피루브산에 의한 저해정도가 낮은 것으로 알려져 있으며 [7], 낮은 온도에 적응하여 서식하는 동물 종일수록 A4 동위효소 의 피루브산에 대한 Michaelis-Menten 상수(Km PYR )값은 증가 한다 [14,17]. 그러므로 LDH A4 동위효소의 역학특성에 관한 실험들은 대사과정에서의 기능을 추정하는데 용이하고, 각 각의 LDH 동위효소들에 대한 항체를 만든다면 환자의 혈액 및 조직에서 빠르게 LDH 동위효소들을 검출 할 수 있으므 로 그 유용성이 매우 크다 [24,26] (Fig.…”