4 resultados para Holbrook
em National Center for Biotechnology Information - NCBI
Resumo:
The crystal structure of the RNA dodecamer 5′-GGCC(GAAA)GGCC-3′ has been determined from x-ray diffraction data to 2.3-Å resolution. In the crystal, these oligomers form double helices around twofold symmetry axes. Four consecutive non-Watson–Crick base pairs make up an internal loop in the middle of the duplex, including sheared G·A pairs and novel asymmetric A·A pairs. This internal loop sequence produces a significant curvature and narrowing of the double helix. The helix is curved by 34° from end to end and the diameter is narrowed by 24% in the internal loop. A Mn2+ ion is bound directly to the N7 of the first guanine in the Watson–Crick region following the internal loop and the phosphate of the preceding residue. This Mn2+ location corresponds to a metal binding site observed in the hammerhead catalytic RNA.
Resumo:
Two outstanding features of the flowering plant family Winteraceae are the occlusion of their stomatal pores by cutin plugs and the absence of water-conducting xylem vessels. An adaptive relationship between these two unusual features has been suggested whereby stomatal plugs restrict gas exchange to compensate for the presumed poor conductivity of their vesselless wood. This hypothesized connection fueled evolutionary arguments that the vesselless condition is ancestral in angiosperms. Here we show that in Drimys winteri, a tree common to wet forests, these stomatal occlusions pose only a small fixed resistance to water loss. In addition, they modify the humidity response of guard cells such that under high evaporative demand, leaves with plugs lose water at a faster rate than leaves from which the plugs have been experimentally removed. Instead of being adaptations for drought, we present evidence that these cuticular structures function to maintain photosynthetic activity under conditions of excess water on the leaf surface. Stomatal plugs decrease leaf wettability by preventing the formation of a continuous water film that would impede diffusion of CO2 into the leaf. Misting of leaves had no effect on photosynthetic rate of leaves with plugs, but resulted in a marked decrease (≈40%) in leaves from which the plugs had been removed. These findings do not support a functional association between stomatal plugs and hydraulic competence and provide a new perspective on debates surrounding the evolution of vessels in angiosperms.
Resumo:
The crystal and molecular structure of an RNA duplex corresponding to the high affinity Rev protein binding element (RBE) has been determined at 2.1-Å resolution. Four unique duplexes are present in the crystal, comprising two structural variants. In each duplex, the RNA double helix consists of an annealed 12-mer and 14-mer that form an asymmetric internal loop consisting of G-G and G-A noncanonical base pairs and a flipped-out uridine. The 12-mer strand has an A-form conformation, whereas the 14-mer strand is distorted to accommodate the bulges and noncanonical base pairing. In contrast to the NMR model of the unbound RBE, an asymmetric G-G pair with N2-N7 and N1-O6 hydrogen bonding, is formed in each helix. The G-A base pairing agrees with the NMR structure in one structural variant, but forms a novel water-mediated pair in the other. A backbone flip and reorientation of the G-G base pair is required to assume the RBE conformation present in the NMR model of the complex between the RBE and the Rev peptide.
Resumo:
We present a method for predicting protein folding class based on global protein chain description and a voting process. Selection of the best descriptors was achieved by a computer-simulated neural network trained on a data base consisting of 83 folding classes. Protein-chain descriptors include overall composition, transition, and distribution of amino acid attributes, such as relative hydrophobicity, predicted secondary structure, and predicted solvent exposure. Cross-validation testing was performed on 15 of the largest classes. The test shows that proteins were assigned to the correct class (correct positive prediction) with an average accuracy of 71.7%, whereas the inverse prediction of proteins as not belonging to a particular class (correct negative prediction) was 90-95% accurate. When tested on 254 structures used in this study, the top two predictions contained the correct class in 91% of the cases.