Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. Abstract Text:

Judy E Kim,Gitrada Arjara,John H Richards,Harry B Gray,Jay R Winkler,

Steady-state and time-resolved fluorescence measurements on each of five native tryptophan residues in full-length and truncated variants of E. coli outer-membrane protein A (OmpA) have been made in folded and denatured states. Tryptophan singlet excited-state lifetimes are multiexponential and vary among the residues. In addition, substantial increases in excited-state lifetimes accompany OmpA folding, with longer lifetimes in micelles than in phospholipid bilayers. This finding suggests that the Trp environments of OmpA folded in micelles and phospholipid bilayers are different. Measurements of Trp fluorescence decay kinetics with full-length OmpA folded in brominated lipid vesicles reveal that W102 is the most distant fluorophore from the hydrocarbon core, while W7 is the closest. Steady-state and time-resolved polarized fluorescence measurements indicate reduced Trp mobility when OmpA is folded in a micelle, and even lower mobility when the protein is folded in a bilayer. The fluorescence properties of truncated OmpA, in which the soluble periplasmic domain is removed, only modestly differ from those of the full-length form, suggesting similar folded structures for the two forms under these conditions.

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. Publishing Authors By Initials

JE Kim,G Arjara,JH Richards,HB Gray,JR Winkler,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The journal of physical chemistry. B

VOLUME: 110

Page Numbers: 17656-62

Journal Abbreviation:

ISSN: 1520-6106

DAY: 7

MONTH: Sep

YEAR: 2006

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101157530

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.

AFFILIATION: Beckman Institute and Department of Chemistry, California Institute of Technology, Pasadena, California 91125, USA.

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Phys Chem B

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence Related Publications

• 3D reconstruction and processing of volumetric data in cryo-electron tomography.
• 3rd International conference on structure, dynamics and function of proteins in biological membranes.
• Alpha-synuclein tertiary contact dynamics.
• An integrated model of group psychotherapy for patients with fibromyalgia.
• Cyclosporin as baseline immunosuppression in solid organ transplantation.
• Equilibrium unfolding of the poly(glutamic acid)20 helix.
• Expanded reverse abdominoplasty for reconstruction of burns in the epigastric region and the inframammary fold in female patients.
• Fixation of the cervical spine using a titanium plate.
• Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6.
• Hedgehog signaling pathway is inactive in colorectal cancer cell lines.
• Heterotopic pregnancy after bilateral salpingectomy resulting in near-term delivery of a healthy infant.
• Image-derived input function for assessment of 18F-FDG uptake by the inflamed lung.
• Josephson effect in hybrid oxide heterostructures with an antiferromagnetic layer.
• Letter: Saline jet-assisted skin graft spreading.
• Mechanism of mRNA destabilization by the glmS ribozyme.
• Microtensile bond strength of resin-resin interfaces after 24-hour and 2-month soaking.
• Multiple cerebral cavernous malformations associated with extracranial mesenchymal anomalies.
• NPHS2 variation in sporadic focal segmental glomerulosclerosis.
• Novel POMGnT1 mutations define broader phenotypic spectrum of muscle-eye-brain disease.
• On the alliinase from garlic: participation of a flavine and inhibition by rotenone.
• Optimization of triarylimidazoles for Tie2: influence of conformation on potency.
• Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.
• Probing the cytochrome c' folding landscape.
• Regulatory polymorphisms in the cyclophilin A gene, PPIA, accelerate progression to AIDS.
• Reprint of "Structural and mechanistic aspects of Amt/Rh proteins" [J. Struct. Biol. 158 (2007) 472-481].
• Site-specific collapse dynamics guide the formation of the cytochrome c' four-helix bundle.
• Structure Analysis of Eukovoside, A New Phenylpropanoid Glycoside from Euphrasia rostkoviana.
• The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins.
• The teleost fish medaka (Oryzias latipes) as genetic model to study gravity dependent bone homeostasis in vivo.
• Two New Secoiridoid Glucosides from Syringa vulgaris.