Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway | Zendy

Hyun-Kyu Choi | Zendy; Duyoung Min | Zendy; Hyunook Kang | Zendy; Min Ju Shon | Zendy; Sang-Hyun Rah | Zendy; Hak Chan Kim | Zendy; Hawoong Jeong | Zendy; HeeJung Choi | Zendy; James U. Bowie | Zendy; TaeYoung Yoon | Zendy

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Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway

Author(s) -

Hyun-Kyu Choi,

Duyoung Min,

Hyunook Kang,

Min Ju Shon,

Sang-Hyun Rah,

Hak Chan Kim,

Hawoong Jeong,

HeeJung Choi,

James U. Bowie,

TaeYoung Yoon

Publication year - 2019

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aaw8208

Subject(s) - membrane protein , rhomboid , folding (dsp implementation) , membrane , biophysics , protein folding , chemistry , integral membrane protein , peripheral membrane protein , crystallography , biology , biochemistry , proteases , enzyme , electrical engineering , engineering

A pathway for helical membrane proteins Membrane proteins are inserted into cell membranes while they are being translated and may fold concurrently into their secondary and tertiary structures. Choiet al. describe a single-molecule force microscopy technique that allowed them to monitor folding of helical membrane proteins in vesicles and bicelles. Two helical membrane proteins, theEscherichia coli rhomboid protease GlpG and the human β2 -adrenergic receptor, both folded from the N to the C terminus, with structures forming in units of helical hairpins. In the cell, this would allow these proteins to begin folding while being translated.Science , this issue p.1150

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