Instability, stabilization, and formulation of liquid protein pharmaceuticals.

A female advantage in school marks is a common finding in education research, and it extends to most course subjects (e.g., language, math, science), unlike what is found on achievement tests. However, questions remain concerning the quantification of these gender differences and the identification of relevant moderator variables. The present meta-analysis answered these questions by examining studies that included an evaluation of gender differences in teacher-assigned school marks in elementary, junior/middle, or high school or at the university level (both undergraduate and graduate). The final analysis was based on 502 effect sizes drawn from 369 samples. A multilevel approach to meta-analysis was used to handle the presence of nonindependent effect sizes in the overall sample. This method was complemented with an examination of results in separate subject matters with a mixed-effects metaanalytic model. A small but significant female advantage (mean d 0.225, 95% CI [0.201, 0.249]) was demonstrated for the overall sample of effect sizes. Noteworthy findings were that the female advantage was largest for language courses (mean d 0.374, 95% CI [0.316, 0.432]) and smallest for math courses (mean d 0.069, 95% CI [0.014, 0.124]). Source of marks, nationality, racial composition of samples, and gender composition of samples were significant moderators of effect sizes. Finally, results showed that the magnitude of the female advantage was not affected by year of publication, thereby contradicting claims of a recent “boy crisis” in school achievement. The present meta-analysis demonstrated the presence of a stable female advantage in school marks while also identifying critical moderators. Implications for future educational and psychological research are discussed.

/pdf/gender-differences-in-scholastic-achievement-a-meta-analysis-5frkycrd3x.pdf

Gender differences in scholastic achievement: a meta-analysis.

Simmerman, Heather K. B., and Larry R. Jones. Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function. Physiol. Rev. 78: 921–947, 1998. — A comprehensive discussion is p...

http://agrino.org/skalifourta/Phospholamban-%20Protein%20Structure,%20Mechanism%20of%20Action,%20and%20Role%20in%20Cardiac%20Function.pdf

Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function

Phase I study of peptide receptor radionuclide therapy with [111In-DTPA0]octreotide: The rotterdam experience

http://www.sciencemadness.org/talk/files.php?pid=304820&aid=26988

Gas explosion handbook

A case history. NMR studies of the structure of a small protein, omega-conotoxin MVIIA.

Binding of a calcium sensitizer, bepridil, to cardiac troponin C. A fluorescence stopped-flow kinetic, circular dichroism, and proton nuclear magnetic resonance study.

A proton nuclear magnetic resonance and molecular modeling study of calmidazolium (R24571) binding to calmodulin and skeletal muscle troponin C.

Introduction to the NMR of proteins

Nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy have been used to characterize the conformation of the putative cytoplasmic domain of phospholamban (PLB), an oligomeric membrane-bound protein which regulates the activity of the cardiac sarcoplasmic reticulum Ca(2+)-dependent ATPase. In aqueous solution the 25-residue peptide adopts a number of rapidly interconverting conformers with no secondary structural type obviously predominating. However, in trifluoroethanol (TFE) the conformation, while still highly dynamic, is characterized by a high proportion of helical structures. Evidence for this is provided by alpha CH chemical shifts and low NH chemical shift temperature coefficients, small NH-alpha CH intraresidue scalar coupling constants, a substantial number of distinctive interresidue nuclear Overhauser effects (NOEs) [dNN(i, i + 1), d alpha N(i, i + 3), d alpha beta(i, i + 3) and d alpha N(i, i + 4)] and characteristic CD bands at 190 (positive), 206 (negative) and 222 nm (negative). The helicity is interrupted around Pro-21. The activity of PLB is regulated by phosphorylation at either Ser-16 or Thr-17. CD shows that phosphorylation at Ser-16 by the cAMP-activated protein kinase causes about an 11% decrease in alpha-helical content in TFE.

Conformation of the cytoplasmic domain of phospholamban by NMR

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