Research Triangle Park

About: Research Triangle Park is a nonprofit organization based out in Durham, North Carolina, United States. It is known for research contribution in the topics: Population & Environmental exposure. The organization has 24961 authors who have published 35800 publications receiving 1684504 citations. The organization is also known as: RTP.

Development and Testing of a Surface Flux and Planetary Boundary Layer Model for Application in Mesoscale Models

Abstract: Although the development of soil, vegetation, and atmosphere interaction models has been driven primarily by the need for accurate simulations of long-term energy and moisture budgets in global climate models, the importance of these processes at smaller scales for short-term numerical weather prediction and air quality studies is becoming more appreciated. Planetary boundary layer (PBL) development is highly dependent on the partitioning of the available net radiation into sensible and latent heat fluxes. Therefore, adequate treatmentof surface properties such as soil moisture and vegetation characteristics is essential for accurate simulation of PBL development, convective and low-level cloud processes, and the temperature and humidity of boundary layer air. In this paper, the development ofa simple coupled surface and PBL model, which is planned for incorporation into the Pennsylvania State University-National Center for Atmospheric Research Mesoscale Model (MM4/5), is described. The soil-vege...

Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain.

Abstract: The endochitinases (E.C. 3.2.1.14, chitinase) are a structurally diverse group of enzymes believed to be important in the biochemical defense of plants against potential pathogens. The gene for a chitinase of Nicotiana tabacum L. cv. Havana 425 has been cloned and sequenced. The major transcription start is 11 bp upstream of the ATG codon and 28 bp downstream of the TATA box. The gene contains two introns and encodes a basic chitinase of 329 amino acids with a 23 amino acid N-terminal signal peptide followed by a 43 amino acid, cysteine-rich domain, which is linked by a hinge region to the main structure of the enzyme. This gene appears to be expressed because the exons are identical to the coding sequence of a cDNA which was isolated. Comparison of chitinase amino acid sequences from different plants indicates there are at least three classes of these enzymes: class I, basic chitinases with an N-terminal cysteine-rich domain and a highly conserved main structure; class II, chitinases similar to the main structure of class I chitinases but lacking the cysteine-rich domain; and, class III, chitinases with conserved sequences different from those of the class I and II enzymes. The sequences encoding the cysteine-rich domain in class I chitinases are flanked by 9-10 bp imperfect direct repeats suggesting that these domains arose from a common ancestral gene and were introduced into genes for class I enzymes by transposition events.

A Nucleic Acid Triple Helix Formed by a Peptide Nucleic Acid-DNA Complex

Abstract: The crystal structure of a nucleic acid triplex reveals a helix, designated P-form, that differs from previously reported nucleic acid structures. The triplex consists of one polypurine DNA strand complexed to a polypyrimidine hairpin peptide nucleic acid (PNA) and was successfully designed to promote Watson-Crick and Hoogsteen base pairing. The P-form helix is underwound, with a base tilt similar to B-form DNA. The bases are displaced from the helix axis even more than in A-form DNA. Hydrogen bonds between the DNA backbone and the Hoogsteen PNA backbone explain the observation that polypyrimidine PNA sequences form highly stable 2:1 PNA-DNA complexes. This structure expands the number of known stable helical forms that nucleic acids can adopt.