A5022600763- Alzheimer's disease research and treatments
- Protein Structure and Dynamics
- Enzyme Structure and Function
- Proteins in Food Systems
- Prion Diseases and Protein Misfolding
- Amyloidosis: Diagnosis, Treatment, Outcomes
- Glycosylation and Glycoproteins Research
- Hemoglobin structure and function
- Supramolecular Self-Assembly in Materials
- Enzyme Production and Characterization
- Parkinson's Disease Mechanisms and Treatments
- Lipid Membrane Structure and Behavior
- Protein Interaction Studies and Fluorescence Analysis
- Monoclonal and Polyclonal Antibodies Research
- Advanced Glycation End Products research
- Reproductive Biology and Fertility
- Animal Genetics and Reproduction
- Protein purification and stability
- Mass Spectrometry Techniques and Applications
- Epigenetics and DNA Methylation
- Molecular spectroscopy and chirality
- RNA and protein synthesis mechanisms
- thermodynamics and calorimetric analyses
- Photosynthetic Processes and Mechanisms
- Drug Transport and Resistance Mechanisms
Osaka University
2016-2025
Meiji University
2021-2023
Toho University
1995-2022
National Agriculture and Food Research Organization
2022
Western Region Agricultural Research Center
2022
Protein Research Foundation
2012-2021
Chubu University
2008-2020
National Livestock Breeding Center
1997-2018
Ministry of Agriculture, Forestry and Fisheries
2018
Hyogo University
2014-2017
Significance Circular dichroism (CD) spectroscopy is widely used for protein secondary structure analysis. However, quantitative estimation β-sheet–containing proteins problematic due to the huge morphological and spectral diversity of β-structures. We show that parallel/antiparallel orientation twisting β-sheets account observed diversity. Taking into twist β-structures, our method accurately estimates a broad range folds, particularly β-sheet–rich amyloid fibrils. Moreover, can predict...
Circular dichroism (CD) spectroscopy is a widely used method to study the protein secondary structure. However, for decades, general opinion was that correct estimation of β-sheet content challenging because large spectral and structural diversity β-sheets. Recently, we showed orientation twisting β-sheets account observed diversity, developed new estimate accurately structure (PNAS, 112, E3095). BeStSel web server provides Beta Structure Selection analyze CD spectra recorded by conventional...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMechanism of acid-induced folding proteinsYuji Goto, Nobuaki Takahashi, and Anthony L. FinkCite this: Biochemistry 1990, 29, 14, 3480–3488Publication Date (Print):April 10, 1990Publication History Published online1 May 2002Published inissue 10 April 1990https://pubs.acs.org/doi/10.1021/bi00466a009https://doi.org/10.1021/bi00466a009research-articleACS PublicationsRequest reuse permissionsArticle Views1367Altmetric-Citations481LEARN ABOUT THESE...
The addition of HCl, at low ionic strength, to the native state apomyoglobin, beta-lactamase, and cytochrome c caused these proteins adopt an essentially fully unfolded conformation in vicinity pH 2. However, contrary expectation, further acid resulted refolding a compact with properties molten globule. major factor responsible for is believed be binding anion, which minimizes intramolecular charge repulsion that initially brought about unfolding.
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTConformational states in .beta.-lactamase: molten-globule at acidic and alkaline pH with high saltYuji Goto Anthony L. FinkCite this: Biochemistry 1989, 28, 3, 945–952Publication Date (Print):February 7, 1989Publication History Published online1 May 2002Published inissue 7 February 1989https://pubs.acs.org/doi/10.1021/bi00429a004https://doi.org/10.1021/bi00429a004research-articleACS PublicationsRequest reuse permissionsArticle...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTClassification of Acid Denaturation Proteins: Intermediates and Unfolded StatesAnthony L. Fink, Linda J. Calciano, Yuji Goto, Takuzo Kurotsu, Daniel R. PallerosCite this: Biochemistry 1994, 33, 41, 12504–12511Publication Date (Print):October 18, 1994Publication History Published online1 May 2002Published inissue 18 October 1994https://pubs.acs.org/doi/10.1021/bi00207a018https://doi.org/10.1021/bi00207a018research-articleACS PublicationsRequest...
Histone modifications play critical roles in the epigenetic regulation of gene expression and maintenance genome integrity. Acetylation methylation histone H3 are particularly important activation silencing. We generated characterized a panel mouse monoclonal antibodies that specifically recognize different on K4, K9, K27 residues H3. By using these for chromatin immunoprecipitation immunoblotting, we analyzed relationship between nearby nucleosomes human cells. Within few nucleosome...
Amyloid fibrils and amorphous aggregates are two types of aberrant associated with protein misfolding diseases. Although they differ in morphology, the forms often treated indiscriminately. β(2)-microglobulin (β2m), a responsible for dialysis-related amyloidosis, amyloid or depending on NaCl concentration at pH 2.5. We compared kinetics their formation, which was monitored by measuring thioflavin T fluorescence, light scattering, 8-anilino-1-naphthalenesulfonate fluorescence. Thioflavin...
Circular dichroism (CD) spectroscopy is widely used to characterize the secondary structure composition of proteins. To derive accurate and detailed structural information from CD spectra, we have developed Beta Structure Selection (BeStSel) method (PNAS, 112, E3095), which can handle spectral diversity β-structured The BeStSel webserver provides this with useful accessories community main goal analyze single or multiple protein spectra. Uniquely, on eight components including parallel...
Among various alcohols, those substituted with fluorine, such as 2,2,2-trifluoroethanol (TFE) or 3,3,3,3',3',3'-hexafluoro-2-propanol (HFIP), have a marked potential to induce the formation of α-helical structures in peptides and denature native proteins. However, mechanism by which these alcohols exert their effects is unknown. Melittin, bee venom peptide, unfolded absence alcohol, but transformed an structure upon addition alcohols. On other hand, β-lactoglobulin, predominantly β-sheet...
Real-time monitoring of fibril growth is essential to clarify the mechanism amyloid formation. Thioflavin T (ThT) a reagent known become strongly fluorescent upon binding fibrils. Here, we show that, by ThT fluorescence with total internal reflection microscopy (TIRFM), fibrils औ2-microgobulin (औ2-m) can be visualized without requiring covalent labeling. One advantages TIRFM would that selectively monitor lying along slide glass, so obtain exact length This method was used follow kinetics...
Alcohols denature the native state of proteins, and also stabilize alpha-helical conformation in unfolded proteins peptides. Among various alcohols, trifluoroethanol (TFE) hexafluoroisopropanol (HFIP) are often used because their high potential to induce such effects. However, reason why TFE HFIP more effective than other alcohols is unknown. Using CD, we studied effects as well reference i.e., methanol, ethanol, isopropanol, on bovine beta-lactoglobulin bee venom melittin at pH 2. Upon...
Understanding the structure and formation of amyloid fibrils, filamentous aggregates proteins peptides, is crucial in preventing diseases caused by their deposition and, moreover, for obtaining further insight into mechanism protein folding misfolding. We have combined solid-state NMR, x-ray fiber diffraction, atomic force microscopy to reveal 3D protofilament-like fibrils formed a 22-residue K3 peptide (Ser(20)-Lys(41)) beta(2)-microglobulin, responsible dialysis-related amyloidosis....
Unfolded states of ribonuclease A were used to investigate the effects macromolecular crowding on compactness and protein folding. The extent folding measured by circular dichroism spectroscopy, fluorescence correlation NMR spectroscopy in presence polyethylene glycol (PEG) or Ficoll as agent. unfolded state RNase a 2.4 M urea solution at pH 3.0 became native conformation addition 35% PEG 20000 70. In addition, inert macromolecule investigated using Fluorescence-labeled test macromolecule....
In β2-microglobulin-related (Aβ2M) amyloidosis, partial unfolding of β2-microglobulin (β2-m) is believed to be prerequisite its assembly into Aβ2M amyloid fibrils in vivo. Although low pH or 2,2,2-trifluoroethanol at a concentration has been reported induce β2-m and subsequent fibril formation vitro, factors that them under near physiological conditions have not determined. Using fluorescence spectroscopy with thioflavin T, circular dichroism spectroscopy, electron microscopy, we here show...