Journal ArticleDOI
Alcohol-induced molten globule intermediates of proteins: are they real folding intermediates or off pathway products?
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TLDR
The results presented in this paper suggest that the molten globule intermediate of proteins in the presence of high alcohols is due to alcohol-induced local folding rather than global folding of unfolded protein and hence is an off-pathway product and not a real folding intermediate.About:
This article is published in Archives of Biochemistry and Biophysics.The article was published on 1998-09-15. It has received 43 citations till now. The article focuses on the topics: Molten globule & Protein folding.read more
Citations
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Journal ArticleDOI
Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein–Ligand Binding
Vijay M. Krishnamurthy,George K. Kaufman,Adam R. Urbach,Irina Gitlin,Katherine L. Gudiksen,Douglas B. Weibel,George M. Whitesides +6 more
TL;DR: Carbonic anhydrase is a protein that is especially well-suited to serve as a model in many types of studies in biophysics, bioanalysis, the physical-organic chemistry of inhibitor design, and medicinal chemistry.
Book ChapterDOI
Role of the molten globule state in protein folding.
Munehito Arai,Kunihiro Kuwajima +1 more
TL;DR: The chapter describes how the molten globule state has been identified as the intermediate of kinetic refolding and discusses the kinetic roles of the molten globeule state in protein folding.
Journal ArticleDOI
Introduction to the Theory and Practice of Fixation of Tissues
TL;DR: The basics of fixation are discussed and the formulas for the fixatives currently used in pathology, histology, and anatomy are provided and good and bad aspects of specific fixatives are discussed.
Journal ArticleDOI
Obtaining antimicrobial peptides by controlled peptic hydrolysis of bovine hemoglobin.
Estelle Yaba Adje,Rafik Balti,Mostafa Kouach,Pascal Dhulster,Didier Guillochon,Naima Nedjar-Arroume +5 more
TL;DR: Twenty-six peptides have an antibacterial activity against Micrococcus luteus, Listeria innocua, and Escherichia coli with MIC from 187.1 to 1 μM and 13 new antibacterial peptides are obtained only in these new hydrolysis conditions.
Journal ArticleDOI
Structure and dynamics of hexafluoroisopropanol-water mixtures by x-ray diffraction, small-angle neutron scattering, NMR spectroscopy, and mass spectrometry
Koji Yoshida,Toshio Yamaguchi,Tomohiro Adachi,Toshiya Otomo,Daisuke Matsuo,Toshiyuki Takamuku,Nobuyuki Nishi +6 more
TL;DR: In this paper, the structure and dynamic properties of aqueous mixtures of 1,1, 1, 3, 3-hexafluoro-2-propanol (HFIP) have been investigated over the whole range of HFIP mole fraction by large-angle x-ray scattering (LAXS), small-angle reutron scattering (SANS), 19F-, 13C-, and 17O-NMR chemical shifts, 17O NMR relaxation, and mass spectrometry.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI
The folding of hen lysozyme involves partially structured intermediates and multiple pathways.
TL;DR: Analysis of the folding of hen lysozyme shows that the protein does not become organized in a single cooperative event but that different parts of the structure become stabilized with very different kinetics.
Journal ArticleDOI
Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding.
TL;DR: It is shown that β-lactoglobulin, which consists predominantly of β-sheets, exhibited a markedly high propensity to form an α–-helical structure in the presence of TFE, as measured by far-UV circular dichroism.
Journal ArticleDOI
A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding.
TL;DR: The effect of 2,2,2-trifluoroethanol (TFE) on the solution conformation of hen egg white lysozyme has been investigated using circular dichroism (CD) and 1H nuclear magnetic resonance (NMR) spectroscopy.
Journal ArticleDOI
Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation.
Paul Thomas,Ken A. Dill +1 more
TL;DR: Comparison with experiments shows that whereas urea as a denaturant is best modeling as weakening both local and nonlocal interactions, trifluoroethanol is best modeled as mainly weakening HH interactions and slightly enhancing local helical interactions.
Related Papers (5)
Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding.
A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding.
Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation.
Paul Thomas,Ken A. Dill +1 more