Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water.

Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water. Research Abstract Details 

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Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water. Abstract Text:

Siegfried ,Benjamin Almeida,Ulrich H E Hansmann,

Parallel temperature molecular dynamics simulations are used to explore the folding of a signal peptide, a short but functionally independent domain at the N-terminus of proteins. The peptide has been analyzed previously by NMR, and thus a solid reference state is provided with the experimental structure. Particular attention is paid to the role of water considered in full atomic detail. Different partial aspects in the folding process are quantified. The major group of obtained structures matches the NMR structure very closely. An important biological consequence is that in vivo folding of signal peptides seems to be possible within aqueous environments.

Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water. Publishing Authors By Initials

S ,B Almeida,UH Hansmann,

For similar water research abstracts see: water research

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Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water. Journal Published:

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

Journal: Proteins

VOLUME: 68

Page Numbers: 662-9

Journal Abbreviation: Proteins

ISSN: 1097-0134

DAY: 15

MONTH: Aug

YEAR: 2007

Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8700181

Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water. Keywords Mesh Terms:

KEYWORDS: Water

MESH TERMS: chemistry

Chemical & Substance for Abstract: Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water. Information

Substance Name: Aldehyde Dehydrogenase

Registry Number: EC 1.2.1.3

Grant and Affiliation Information for Parallel tempering molecular dynamics folding simulation of a signal peptide in explicit water.

AFFILIATION: Department of Physics, Michigan Technological University, Houghton, Michigan 49331-1295, USA. shoefing@mtu.edu

Country: United States

AGENCY: United States NIGMS

GRANT: GM62838

ACRONYM: GM

MEDLINETA: Proteins

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