Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates-Reference-Cited by-同舟云学术

Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates

Published:1995-08 Issue:8 Volume:4 Page:1553-1562
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Sci.

Author:

Engelhard Markus,Evans Philip A.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference26 articles.

1. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin;Baum;Biochemistry,1989

2. Kinetic resolution of peptide bond and sidechain far-UV circular dichroism during the folding of hen egg white lysozyme;Chaffotte;Biochemistry,1992

3. The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS;Cocco;Protein Sci,1994

4. Compact state of a protein with pronounced small scale mobility: Bovine α-lactalbumin;Dolgikh;Eur Biophys J,1985

5. Probing the structure of folding intermediates;Evans;Curr Opin Struct Biol,1994

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