منابع مشابه
Helical membrane protein folding, stability, and evolution.
Helical membrane protein folding and oligomerization can be usefully conceptualized as involving two energetically distinct stages-the formation and subsequent side-to-side association of independently stable transbilayer helices. The interactions of helices with the bilayer, with prosthetic groups, and with each other are examined in the context of recent evidence. We conclude that the two-sta...
متن کاملKinetics and Thermodynamics of Membrane Protein Folding
Understanding protein folding has been one of the great challenges in biochemistry and molecular biophysics. Over the past 50 years, many thermodynamic and kinetic studies have been performed addressing the stability of globular proteins. In comparison, advances in the membrane protein folding field lag far behind. Although membrane proteins constitute about a third of the proteins encoded in k...
متن کاملMembrane protein folding makes the transition.
T he study of the folding of membrane proteins has lagged far behind that of small soluble proteins—yet proteins that reside within biological membranes account for approximately a third of all proteomes. The article by Huysmans et al. in this issue of PNAS (1) represents a breakthrough by reporting a comprehensive φ-value analysis of the folding of a membrane protein (i.e., PagP) into a lipid ...
متن کاملMembrane protein folding and stability: physical principles.
Stably folded membrane proteins reside in a free energy minimum determined by the interactions of the peptide chains with each other, the lipid bilayer hydrocarbon core, the bilayer interface, and with water. The prediction of three-dimensional structure from sequence requires a detailed understanding of these interactions. Progress toward this objective is summarized in this review by means of...
متن کاملMembrane Defects Accelerate Outer Membrane β-Barrel Protein Folding
Outer membrane β-barrel proteins spontaneously fold into lipid bilayers with rates of folding that are strongly influenced by the physical properties of the membrane. We show that folding is accelerated when the bilayer is at the phase transition temperature, because of the coexistence of lipid phase domains and the high degree of defects present at domain boundaries. These results are consiste...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2015
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2014.11.265