Non-native α-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin-Reference-Cited by-同舟云学术

Non-native α-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin

Published:2009-07 Issue:1 Volume:76 Page:226-236
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Tsukamoto Seiichi,Yamashita Takako,Yamada Yoshiteru,Fujiwara Kazuo,Maki Kosuke,Kuwajima Kunihiro,Matsumura Yoshitaka,Kihara Hiroshi,Tsuge Hideaki,Ikeguchi Masamichi

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

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4. Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C2221. Structural differences between genetic variants A and B and features of the Tanford transition;Oliveira;Eur J Biochem,2001

5. A novel pH-dependent dimerization motif in β-lactoglobulin from pig (Sus scrofa);Hoedemaeker;Acta Crystallogr D Biol Crystallogr,2002

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1. Non-Native α-Helices in the Initial Folding Intermediate Facilitate the Ordered Assembly of the β-Barrel in β-Lactoglobulin;Biochemistry;2017-08-31

2. The Non-native Helical Intermediate State May Accumulate at Low pH in the Folding and Aggregation Landscape of the Intestinal Fatty Acid Binding Protein;Biochemistry;2016-08-04

3. Effect of non-native helix destabilization on the folding of equine β-lactoglobulin;The Journal of Biochemistry;2014-06-18

4. Delineation of Solution Burst-Phase Protein Folding Events by Encapsulating the Proteins in Silica Gels;Biochemistry;2014-06-05

5. Relationship between chain collapse and secondary structure formation in a partially folded protein;Biopolymers;2014-03-25