Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.

Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Abstract Text:

Jae-Hyun Cho,Satoshi Sato,Jia-Cherng Horng,Burcu Anil,Daniel P Raleigh,Jae-Hyun Cho,Satoshi Sato,Jia-Cherng Horng,Burcu Anil,Daniel P Raleigh,

It is now recognized that the denatured state ensemble (DSE) of proteins can contain significant amounts of structure, particularly under native conditions. Well-studied examples include small units of hydrogen bonded secondary structure, particularly helices or turns as well as hydrophobic clusters. Other types of interactions are less well characterized and it has often been assumed that electrostatic interactions play at most a minor role in the DSE. However, recent studies have shown that both favorable and unfavorable electrostatic interactions can be formed in the DSE. These can include surprisingly specific non-native interactions that can even persist in the transition state for protein folding. DSE electrostatic interactions can be energetically significant and their modulation either by mutation or by varying solution conditions can have a major impact upon protein stability. pH dependent stability studies have shown that electrostatic interactions can contribute up to 4 kcal mol(-1) to the stability of the DSE.

Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Publishing Authors By Initials

JH Cho,S Sato,JC Horng,B Anil,DP Raleigh,JH Cho,S Sato,JC Horng,B Anil,DP Raleigh,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Journal Published:

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

Journal: Archives of biochemistry and biophysics

VOLUME: 469

Page Numbers: 20-8

Journal Abbreviation: Arch. Biochem. Biophys.

ISSN: 1096-0384

DAY: 22

MONTH: 08

YEAR: 2007

Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372430

Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.

AFFILIATION: Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. Jc2980@columbia.edu

Country: United States

AGENCY: United States NIGMS

GRANT: GM 70941

ACRONYM: GM

MEDLINETA: Arch Biochem Biophys

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability 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.