Stable folding core in the folding transition state of an -helical integral membrane protein
نویسندگان
چکیده
منابع مشابه
Stable folding core in the folding transition state of an α-helical integral membrane protein
Defining the structural features of a transition state is important in understanding a folding reaction. Here, we use Φ-value and double mutant analyses to probe the folding transition state of the membrane protein bacteriorhodopsin. We focus on the final C-terminal helix, helix G, of this seven transmembrane helical protein. Φ-values could be derived for 12 amino acid residues in helix G, most...
متن کاملThe transition state for integral membrane protein folding.
Biology relies on the precise self-assembly of its molecular components. Generic principles of protein folding have emerged from extensive studies on small, water-soluble proteins, but it is unclear how these ideas are translated into more complex situations. In particular, the one-third of cellular proteins that reside in biological membranes will not fold like water-soluble proteins because m...
متن کاملThe transition state for folding of an outer membrane protein.
Inspired by the seminal work of Anfinsen, investigations of the folding of small water-soluble proteins have culminated in detailed insights into how these molecules attain and stabilize their native folds. In contrast, despite their overwhelming importance in biology, progress in understanding the folding and stability of membrane proteins remains relatively limited. Here we use mutational ana...
متن کاملHelical 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 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 کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2011
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1012594108