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A protein sequence that can encode native structure by disfavoring alternate conformations

Authors
 W. Christian Wigley  ;  Michael J. Corboy  ;  Todd D. Cutler  ;  Patrick H. Thibodeau  ;  Jorge Oldan  ;  Min Goo Lee  ;  Josep Rizo  ;  John F. Hunt  ;  Philip J. Thomas 
Citation
 NATURE STRUCTURAL BIOLOGY , Vol.9(5) : 381-388, 2002 
Journal Title
 NATURE STRUCTURAL BIOLOGY 
ISSN
 1072-8368 
Issue Date
2002
MeSH
Amino Acid Sequence ; Cell Line ; Cell Membrane/metabolism ; Circular Dichroism ; Computational Biology ; Cystic Fibrosis Transmembrane Conductance Regulator/chemistry* ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism* ; Genome ; Humans ; Liposomes/metabolism ; Micelles ; Molecular Sequence Data ; Mutation/genetics ; Proline/genetics ; Proline/metabolism* ; Protein Folding* ; Protein Structure, Secondary ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Spectroscopy, Fourier Transform Infrared ; Structure-Activity Relationship ; Thermodynamics ; Thiazoles/metabolism
Abstract
The linear sequence of amino acids contains all the necessary information for a protein to fold into its unique three-dimensional structure. Native protein sequences are known to accomplish this by promoting the formation of stable, kinetically accessible structures. Here we describe a Pro residue in the center of the third transmembrane helix of the cystic fibrosis transmembrane conductance regulator that promotes folding by a distinct mechanism: disfavoring the formation of a misfolded structure. The generality of this mechanism is supported by genome-wide transmembrane sequence analyses. Furthermore, the results provide an explanation for the increased frequency of Pro residues in transmembrane alpha-helices. Incorporation by nature of such 'negative folding determinants', aimed at preventing the formation of off-pathway structures, represents an additional mechanism by which folding information is encoded within the evolved sequences of proteins.
Full Text
http://www.nature.com/nsmb/journal/v9/n5/full/nsb784.html
DOI
10.1038/nsb784
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers
Yonsei Authors
Lee, Min Goo(이민구) ORCID logo https://orcid.org/0000-0001-7436-012X
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/143465
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