NDLI: Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.

Please wait, while we are loading the content...

Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area.

Free energies of protein decoys provide insight into determinants of protein stability.

Substitution rates in alpha-helical transmembrane proteins.

The role of strand 1 of the C β-sheet in the structure and function of $α_{1}-antitrypsin$

Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.

pH-induced folding of an apoptotic coiled coil.

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.

Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms.

Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection.

Antifreeze protein from shorthorn sculpin: identification of the ice-binding surface.

Molecular design of Mycoplasma hominis Vaa adhesin.

Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.

Catalytic and binding poly-reactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution.

The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.

Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor

Surface interactions in the complex between cytochrome f and the E43Q/D44N and E59K/E60Q plastocyanin double mutants as determined by (1)H-NMR chemical shift analysis.

Preferred proline puckerings in cis and trans peptide groups: implications for collagen stability.

Year: 2001 Volume: 10 Issue: 11

Year: 2001 Volume: 10 Issue: 10

Year: 2001 Volume: 10 Issue: 9

Year: 2001 Volume: 10 Issue: 8

Year: 2001 Volume: 10 Issue: 7

Year: 2001 Volume: 10 Issue: 6

Year: 2001 Volume: 10 Issue: 5

Year: 2001 Volume: 10 Issue: 4

Year: 2001 Volume: 10 Issue: 3

Year: 2001 Volume: 10 Issue: 2

Year: 2001 Volume: 10 Issue: 1

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dobson, C. M. Chiti, F. Taddei, N. Bucciantini, M. Stefani, M. Capanni, C.
Description	Country affiliation: Italy Author Affiliation: Chiti F ( Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy.)
Abstract	The HypF N-terminal domain has been found to convert readily from its native globular conformation into protein aggregates with the characteristics of amyloid fibrils associated with a variety of human diseases. This conversion was achieved by incubation at acidic pH or in the presence of moderate concentrations of trifluoroethanol. Electron microscopy showed that the fibrils grown in the presence of trifluoroethanol were predominantly 3-5 nm and 7-9 nm in width, whereas fibrils of 7-9 nm and 12-20 nm in width prevailed in samples incubated at acidic pH. These results indicate that the assembly of protofilaments or narrow fibrils into mature amyloid fibrils is guided by interactions between hydrophobic residues that may remain exposed on the surface of individual protofilaments. Therefore, formation and isolation of individual protofilaments appears facilitated under conditions that favor the destabilization of hydrophobic interactions, such as in the presence of trifluoroethanol.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	12
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Beta-peptides Chemistry Amyloid Bacterial Proteins Genetics Circular Dichroism Cloning, Molecular Coloring Agents Pharmacology Congo Red Escherichia Coli Metabolism Fluorescent Dyes Hot Temperature Hydrogen-ion Concentration Microscopy, Electron Protein Structure, Tertiary Thiazoles Time Factors Trifluoroethanol Urea Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain

Formation of amyloid fibrils by bovine carbonic anhydrase

Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH

Congo red dichroism with dispersed amyloid fibrils, an extrinsic cotton effect.

Amyloid fibril formation in vitro from halophilic metal binding protein: its high solubility and reversibility minimized formation of amorphous protein aggregations.

Molecules of Congo red caught hopping between insulin fibrils: a chiroptical probe of the dye–amyloid binding dynamics

Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.

Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.

Chaperone-like activity of heme group against amyloid-like fibril formation by hen egg ovalbumin: possible mechanism of action.

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.

Similar Documents

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain

Formation of amyloid fibrils by bovine carbonic anhydrase

Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH

Congo red dichroism with dispersed amyloid fibrils, an extrinsic cotton effect.

Amyloid fibril formation in vitro from halophilic metal binding protein: its high solubility and reversibility minimized formation of amorphous protein aggregations.

Molecules of Congo red caught hopping between insulin fibrils: a chiroptical probe of the dye–amyloid binding dynamics

Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.

Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.

Chaperone-like activity of heme group against amyloid-like fibril formation by hen egg ovalbumin: possible mechanism of action.

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.