Document Detail

Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer.
MedLine Citation:
PMID:  17416618     Owner:  NLM     Status:  MEDLINE    
We demonstrate that the sub-millisecond protein folding process referred to as "collapse" actually consists of at least two separate processes. We observe the UV fluorescence spectrum from naturally occurring tryptophans in three well-studied proteins, cytochrome c, apomyoglobin, and lysozyme, as a function of time in a microfluidic mixer with a dead time of approximately 20 mus. Single value decomposition of the time-dependent spectra reveal two separate processes: 1), a spectral shift which occurs within the mixing time; and 2), a fluorescence decay occurring between approximately 100 and 300 micros. We attribute the first process to hydrophobic collapse and the second process to the formation of the first native tertiary contacts.
Lisa J Lapidus; Shuhuai Yao; Kimberly S McGarrity; David E Hertzog; Emily Tubman; Olgica Bakajin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-04-06
Journal Detail:
Title:  Biophysical journal     Volume:  93     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  2007 Jul 
Date Detail:
Created Date:  2007-06-07     Completed Date:  2007-08-01     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  218-24     Citation Subset:  IM    
Department of Physics and Astronomy, Michigan State University, East Lansing, Michigan, USA.
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MeSH Terms
Microfluidics / methods*
Models, Chemical*
Models, Molecular*
Protein Conformation
Protein Denaturation
Protein Folding*
Proteins / chemistry*,  ultrastructure*
Reg. No./Substance:

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