The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9.

The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Abstract Text:

Ying Li,Bing Shan,Daniel P Raleigh,

A point mutation of a small globular protein, the C-terminal domain of L9 destabilizes the protein and leads to observable cold-denaturation at temperatures above zero. The cold denatured state is in slow exchange with the native state on the NMR time scale, and this allows the hydrodynamic properties of the cold unfolded state and the native state to be measured under identical conditions using pulsed-field gradient NMR diffusion measurements. This provides the first experimental measurement of the hydrodynamic properties of a cold unfolded protein and its folded form under identical conditions. Hydrodynamic radii of the cold-induced unfolded states were measured for a set of temperatures ranging from 2 degrees C to 25 degrees C at pD 6.6 in the absence of denaturant. The cold unfolded state is compact compared to the urea or acid unfolded state and a trend of increasing radii of hydration is observed as the temperature is lowered. These observations are confirmed by experiments on the same protein at pD 8.0, where it is more stable, in the presence of a modest concentration of urea. The expansion of the cold-denatured state at lower temperatures is consistent with the temperature dependence of hydrophobic interactions.

The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Publishing Authors By Initials

Y Li,B Shan,DP Raleigh,

For similar natural sciences: physics: thermodynamics research abstracts see: natural sciences: physics: thermodynamics research

PUBMED ID PMID:

MEDLINE DATE:

The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of molecular biology

VOLUME: 368

Page Numbers: 256-62

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 11

MONTH: 02

YEAR: 2007

The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Keywords Mesh Terms:

KEYWORDS: Thermodynamics

MESH TERMS: genetics

Chemical & Substance for Abstract: The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. Information

Substance Name: Isoleucine

Registry Number: 73-32-5

Grant and Affiliation Information for The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9.

AFFILIATION: Department of Chemistry, State University of New York at Stony Brook, Stony Brook, NY 11794-3400, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM 70941

ACRONYM: GM

MEDLINETA: J Mol Biol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9 Related Publications

• A simple and economical method for the production of 13C,18O-labeled Fmoc-amino acids with high levels of enrichment: applications to isotope-edited IR studies of proteins.
• Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology.
• Care quality data is too hard to pin down.
• Collection of data on ethnic origin in England.
• Denatured state effects and the origin of nonclassical phi values in protein folding.
• Design of a hyperstable protein by rational consideration of unfolded state interactions.
• Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
• Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.
• Equality. Big Brother isn't watching you.
• Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability.
• Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation.
• Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9.
• Mitochondrial content of choroid plexus epithelium.
• My journey in nursing.
• Pill or people?--the choice is ours.
• Rifampicin Does Not Prevent Amyloid Fibril Formation by Human Islet Amyloid Polypeptide but Does Inhibit Fibril Thioflavin-T Interactions: Implications for Mechanistic Studies of beta-Cell Death.
• Temperature-dependent hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects.
• The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9.
• The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation.
• The use of mice in experimental chemotherapy of tuberculosis; the histopathologic assay of chemotherapeutic action.
• Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.
• phi-Values beyond the ribosomally encoded amino acids: kinetic and thermodynamic consequences of incorporating trifluoromethyl amino acids in a globular protein.