De novo Refolding and Aggregation of Insulin in a Nonaqueous Environment: An Inside out Protein Remake-Reference-Cited by-同舟云学术

De novo Refolding and Aggregation of Insulin in a Nonaqueous Environment: An Inside out Protein Remake

Published:2008-06-26 Issue:29 Volume:112 Page:8744-8747
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Fulara Aleksandra¹,Wojcik Sławomir¹,Loksztejn Anna¹,Dzwolak Wojciech¹

Affiliation:

1. Institute of High Pressure Physics, Polish Academy of Sciences, Sokolowska 29/37, 01-142 Warsaw, Poland, and Department of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp8029727

Reference23 articles.

1. Ethanol-Perturbed Amyloidogenic Self-Assembly of Insulin: Looking for Origins of Amyloid Strains

2. Principles that Govern the Folding of Protein Chains

3. The Diastereomeric Assembly of Polylysine Is the Low-Volume Pathway for Preferential Formation of β-Sheet Aggregates

4. Alternative Membrane Protein Conformations in Alcohols

5. Thermodynamic Properties Underlying the α-Helix-to-β-Sheet Transition, Aggregation, and Amyloidogenesis of Polylysine as Probed by Calorimetry, Densimetry, and Ultrasound Velocimetry

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