Works (7)

Updated: July 5th, 2023 15:59

2006 journal article

Analysis of ESTs from multiple Gossypium hirsutum tissues and identification of SSRs

GENOME, 49(4), 306–319.

By: E. Taliercio*, R. Allen, M. Essenberg, N. Klueva, H. Nguyen, M. Patil, P. Payton, A. Millena ...

author keywords: drought stress; gene annotation; gene mapping; tentative consensus sequence (TC); Xanthomonas campestris
MeSH headings : Chromosome Mapping / methods; Consensus Sequence / genetics; Databases, Nucleic Acid; Expressed Sequence Tags / chemistry; Gene Library; Genes, Plant; Genetic Linkage; Genetic Markers; Gossypium / genetics; Minisatellite Repeats / genetics; Plant Structures / genetics; Plant Structures / microbiology; Polymorphism, Genetic; Xanthomonas campestris / pathogenicity
TL;DR: In an effort to expand the Gossypium hirsutum L. (cotton) expressed sequence tag (EST) database, ESTs representing a variety of tissues and treatments were sequenced and simple sequence repeats (SSRs) were identified, and an inexpensive method was developed to screen genomic DNA for the presence of these SSRs. (via Semantic Scholar)
UN Sustainable Development Goal Categories
2. Zero Hunger (Web of Science)
13. Climate Action (Web of Science)
Source: Web Of Science
Added: August 6, 2018

2006 review

Spontaneous fibril formation by polyalanines; Discontinuous molecular dynamics simulations

[Review of ]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 128(6), 1890–1901.

By: H. Nguyen n & C. Hall n

MeSH headings : Amyloid / chemistry; Computer Simulation; Hydrophobic and Hydrophilic Interactions; Kinetics; Models, Molecular; Peptides / chemistry; Protein Structure, Secondary; Temperature; Thermodynamics
TL;DR: This work investigates the formation of fibrils by performing discontinuous molecular dynamics simulations on systems containing 12 to 96 model Ac-KA(14)K-NH(2) peptides using the newly developed PRIME model, which finds that, at a low concentration, random-coil peptides assemble into alpha-helices at low temperatures. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2005 journal article

Kinetics of fibril formation by polyalanine peptides

JOURNAL OF BIOLOGICAL CHEMISTRY, 280(10), 9074–9082.

By: H. Nguyen n & C. Hall n

MeSH headings : Amyloid / chemistry; Amyloid / ultrastructure; Computer Simulation; Models, Molecular; Peptides; Protein Conformation
TL;DR: It is found that fibril formation for polyalanines incorporate features that are characteristic of three models, the templated assembly, nucleated polymerization, and nucleated conformational conversion models, but that none of them gave a completely satisfactory description of the simulation kinetics. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2004 journal article

Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 101(46), 16180–16185.

By: H. Nguyen n & C. Hall n

author keywords: amyloid; protein aggregation
MeSH headings : Amyloid / chemistry; Biophysical Phenomena; Biophysics; Humans; In Vitro Techniques; Models, Molecular; Multiprotein Complexes; Peptides / chemistry; Thermodynamics
TL;DR: Systems containing 12-96 model polyalanine peptides form fibrils at temperatures greater than a critical temperature that decreases with peptide concentration and exceeds the peptide's folding temperature, consistent with experimental findings. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2004 journal article

Phase diagrams describing fibrillization by polyalanine peptides

BIOPHYSICAL JOURNAL, 87(6), 4122–4134.

By: H. Nguyen n & C. Hall n

MeSH headings : Amyloid / chemistry; Binding Sites; Computer Simulation; Dimerization; Models, Chemical; Models, Molecular; Multiprotein Complexes / chemistry; Peptides / chemistry; Phase Transition; Protein Binding; Protein Conformation; Temperature
TL;DR: The thermodynamics of fibril formation is examined using the newly-developed off-lattice intermediate-resolution protein model, PRIME, which is simple enough to allow the treatment of large multichain systems while maintaining a fairly realistic description of protein dynamics when used in conjunction with constant-temperature discontinuous molecular dynamics. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2004 journal article

Solvent effects on the conformational transition of a model polyalanine peptide

Protein Science, 13(11), 2909–2924.

By: H. Nguyen n, A. Marchut n & C. Hall n

author keywords: polyalanine; alpha-beta transition; secondary structures; solvent conditions; discontinuous molecular dynamics
MeSH headings : Hydrogen Bonding / drug effects; Models, Molecular; Peptides / chemistry; Protein Structure, Secondary / drug effects; Solvents / pharmacology; Temperature
TL;DR: A study of the folding of a single polyalanine‐based peptide is investigated by combining discontinuous molecular dynamics simulation with the newly developed off‐lattice intermediate‐resolution protein model, setting the stage for a study of polyalanines aggregation in a forthcoming paper. (via Semantic Scholar)
Sources: Web Of Science, Crossref, NC State University Libraries
Added: August 6, 2018

2002 journal article

Effect of rate of chemical or thermal renaturation on refolding and aggregation of a simple lattice protein

BIOTECHNOLOGY AND BIOENGINEERING, 80(7), 823–834.

By: H. Nguyen n & C. Hall n

author keywords: protein folding; protein aggregation; renaturation; Monte Carlo; computer simulation
MeSH headings : Computer Simulation; Macromolecular Substances; Models, Chemical; Models, Molecular; Monte Carlo Method; Protein Conformation; Protein Folding; Protein Renaturation; Proteins / chemistry; Sensitivity and Specificity; Temperature
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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