Teacher Perception and Their Understanding of Progress Monitoring Throughout a Longitudinal Assessment System

The purpose of this qualitative study was to examine the phenomenon of teacher perception and their understanding of progress monitoring throughout a longitudinal assessment system. This monitoring of student progress is to enhance their academic skills in mathematics and provide necessary interventions for growth as measured on a longitudinal assessment system through fidelity of implementation of interventions processed through progress monitoring. Data was collected from participant responses through interviews, a demographic survey, and focus groups. Interview respondents participated in a closed-door, face-to-face interview. The survey was used to collect specific demographic data to provide a concise snapshot of each individual teacher. From the interviews, four major themes and 13 sub-themes emerged from 302 codes. Focus group respondents participated in a closed door, small group setting that concentrated on a single, open-ended question. From the focus groups, three major themes and nine sub-themes emerged from an average of 26 codes per group. Analysis of the themes captured a collage of personal responses from participants. Participants’ shared perceptions of progress monitoring that varied from each other to the extent that some believed it was synonymous with grading assignments and not actually monitoring the progress of academic growth and skill mastery. Moreover, this led to the teacher belief that there was a need for professional development, training and open communication with other math teachers and educational support staff. Participants also identified a gap in student understanding of progress monitoring and the root purpose for longitudinal assessments. Participants also believed students should be a part of their own learning and progress monitoring. A web of connections recognized need and want for progress monitoring. Finally, the shared perceptions in this study presented an avenue for continued conversation within the district of study and other educational communities - conversations that must continue until students are making adequate growth

Lysine: N 6 -Hydroxylase: Stability and Interaction with Ligands

Recombinant lysine:N 6 -hydroxylase, r IucD, which is isolated as an apoenzyme, requires FAD and NADPH for its catalytic function. r IucD preparations have been found to undergo time-dependent loss in monooxygenase function due to aggregation from the initial tetrameric state to a polytetrameric form(s), a process which is reversible by treatment with thiols. Ligand-in-duced conformational changes in r IucD were assessed by monitoring its CD spectra, DSC profile, and susceptibility to both endo- as well as exopeptidases. The first two methods indicated the absence of any significant conformational change in r IucD, while the last approach revealed that FAD, and its analog ADP, can protect the protein from the deleterious action of proteases. NADPH was partially effective and L-lysine was ineffective in this regard. Deletion of the C-terminal segment, either by treatment with carboxypeptidase Y or by mutagenesis of iucD, results in the loss of r IucD's monooxygenase activity. These findings demonstrate the crucial role of the C-terminal segment in maintaining r IucD in its native conformation.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/45085/1/10930_2004_Article_409465.pd

CONTROL ROD DRIVE PROTO-TYPE TEST REPORT

An evaluation under simulated Pathfinder reactor operating conditions of a prototype Pathfinder control rod drive (described) indicated that the unit will perform satisfactorily under all Pathfinder operating conditions. Tests were performed on individual components of the drive and on the assembled drive. (D.C.W.

Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme

Phage lambda lysozyme is structurally related to other known lysozymes but its mechanism of action is different from the classical lysozyme mechanism, acting as a transglycosidase rather than a hydrolase. As two conformations have been revealed by the crystal structure, we investigated the effect of mutating and modifying a histidine located near to or far from the active site in the respective closed and open conformations. Whereas its asparagine mutation has little or no effect on activity, its N-carbethoxylation inactivates the enzyme. This provide further evidence for the involvement of the closed conformation and for the need of conformational mobility in lambda lysozyme function

Fluorine: A new element in protein design

Fluorocarbons are quintessentially man‐made molecules, fluorine being all but absent from biology. Perfluorinated molecules exhibit novel physicochemical properties that include extreme chemical inertness, thermal stability, and an unusual propensity for phase segregation. The question we and others have sought to answer is to what extent can these properties be engineered into proteins? Here, we review recent studies in which proteins have been designed that incorporate highly fluorinated analogs of hydrophobic amino acids with the aim of creating proteins with novel chemical and biological properties. Fluorination seems to be a general and effective strategy to enhance the stability of proteins, both soluble and membrane bound, against chemical and thermal denaturation, although retaining structure and biological activity. Most studies have focused on small proteins that can be produced by peptide synthesis as synthesis of large proteins containing specifically fluorinated residues remains challenging. However, the development of various biosynthetic methods for introducing noncanonical amino acids into proteins promises to expand the utility of fluorinated amino acids in protein design.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/90596/1/2030_ftp.pd

Large-scale mapping of human protein–protein interactions by mass spectrometry

Mapping protein–protein interactions is an invaluable tool for understanding protein function. Here, we report the first large-scale study of protein–protein interactions in human cells using a mass spectrometry-based approach. The study maps protein interactions for 338 bait proteins that were selected based on known or suspected disease and functional associations. Large-scale immunoprecipitation of Flag-tagged versions of these proteins followed by LC-ESI-MS/MS analysis resulted in the identification of 24 540 potential protein interactions. False positives and redundant hits were filtered out using empirical criteria and a calculated interaction confidence score, producing a data set of 6463 interactions between 2235 distinct proteins. This data set was further cross-validated using previously published and predicted human protein interactions. In-depth mining of the data set shows that it represents a valuable source of novel protein–protein interactions with relevance to human diseases. In addition, via our preliminary analysis, we report many novel protein interactions and pathway associations

The Contribution of Coevolving Residues to the Stability of KDO8P Synthase

The evolutionary tree of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase (KDO8PS), a bacterial enzyme that catalyzes a key step in the biosynthesis of bacterial endotoxin, is evenly divided between metal and non-metal forms, both having similar structures, but diverging in various degrees in amino acid sequence. Mutagenesis, crystallographic and computational studies have established that only a few residues determine whether or not KDO8PS requires a metal for function. The remaining divergence in the amino acid sequence of KDO8PSs is apparently unrelated to the underlying catalytic mechanism.The multiple alignment of all known KDO8PS sequences reveals that several residue pairs coevolved, an indication of their possible linkage to a structural constraint. In this study we investigated by computational means the contribution of coevolving residues to the stability of KDO8PS. We found that about 1/4 of all strongly coevolving pairs probably originated from cycles of mutation (decreasing stability) and suppression (restoring it), while the remaining pairs are best explained by a succession of neutral or nearly neutral covarions.Both sequence conservation and coevolution are involved in the preservation of the core structure of KDO8PS, but the contribution of coevolving residues is, in proportion, smaller. This is because small stability gains or losses associated with selection of certain residues in some regions of the stability landscape of KDO8PS are easily offset by a large number of possible changes in other regions. While this effect increases the tolerance of KDO8PS to deleterious mutations, it also decreases the probability that specific pairs of residues could have a strong contribution to the thermodynamic stability of the protein