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The activity of the muscletype Torpedo nicotinic acetylcholine receptor nAChR is highly sensitive to lipids but the underlying mechanisms remain poorly understood The nAChR transmembrane αhelix M4 is positioned at the perimeter of each subunit in direct contact with lipids and likely plays a central role in lipidsensing To gain insight into the mechanisms underlying nAChR lipidsensing we use homology modeling coevolutionary analyses sitedirected mutagenesis and electrophysiology to examine the role of the αsubunit M4 αM4 in the function of the adult muscle nAChR Ala substitutions of most αM4 residues including those in clusters of polar residues at both the N and C termini and deletion of up to 11 Cterminal residues had little impact on the agonistinduced response Even Ala substitutions of coevolved pairs of residues at the interface between αM4 and the adjacent helices αM1 and αM3 had little effect although some impaired nAChR expression On the other hand Ala substitutions of Thr422 and Arg429 caused relatively large losses of function suggesting functional roles for these specific residues Ala substitutions of aromatic residues at the αM4αM1αM3 interface generally led to gains of function as previously reported for the prokaryotic homolog the Erwinia chrysanthemi ligandgated ion channel ELIC The functional effects of individual Ala substitutions in αM4 were found to be additive although not in a completely independent manner Our results provide insight into the structural features of αM4 that are important They also suggest how lipid dependent changes in αM4 structure may ultimately modify nAChR functionCells have a remarkable ability to synthesize large amounts of protein in a very short period of time Under these conditions many hydrophobic surfaces on proteins may be transiently exposed and the likelihood of deleterious interactions is quite high To counter this threat to cell viability molecular chaperones have evolved to help nascent polypeptides fold correctly and multimeric protein complexes assemble productively while minimizing the danger of protein aggregation Heat shock protein 90 Hsp90 is an evolutionarily conserved molecular chaperone that is involved in the stability and activation of at least 300 proteins also known as clients under normal cellular conditions The Hsp90 clients participate in the full breadth of cellular processes including cell growth and cell cycle control signal transduction DNA repair transcription and many others Hsp90 chaperone function is coupled to its ability to bind and hydrolyze ATP which is tightly regulated both by cochaperone proteins and posttranslational modifications PTMs Many reported PTMs of Hsp90 alter chaperone function and consequently affect myriad cellular processes Here we review the contributions of PTMs such as phosphorylation acetylation SUMOylation methylation OGlcNAcylation ubiquitination and others towards regulation of Hsp90 function We also discuss how the Hsp90 modification state affects cellular sensitivity to Hsp90targeted therapeutics that specifically bind and inhibit its chaperone activity The ultimate challenge is to decipher the comprehensive and combinatorial array of PTMs that modulate Hsp90 chaperone function a phenomenon termed the chaperone codeThe National Science Foundation estimates that 80 of the jobs available during the next decade will require math and science skills dictating that programs in biochemistry and molecular biology must be transformative and use new pedagogical approaches and experiential learning for careers in industry research education engineering healthcare professions and other interdisciplinary fields These efforts require an environment that values the individual student integrates recent advances from the primary literature in the discipline experimentally directed research data collection and analysis and scientific writing Current trends shaping these efforts must include critical thinking experimental testing computational modeling and inferential logic In essence modern biochemistry and molecular biology education must be informed by and integrated with cuttingedge research This environment relies on sustained research support commitment to provide the requisite mentoring access to instrumentation and stateoftheart facilities The academic environment must establish a culture of excellence and faculty engagement leading to innovation in the classroom and laboratory These efforts must not lose sight of the importance of multidimensional programs that enrich science literacy in all facets of the population students and teachers in K12 schools nonbiochemistry and molecular biology students and other stakeholders As biochemistry and molecular biology educators we have an obligation to provide students with the skills that allow them to be innovative and selfreliant Trichostatin A mw The next generation of biochemistry and molecular biology students must be taught proficiencies in scientific and technological literacy the importance of the scientific discourse and skills required for problem solvers of the 21st centuryLLysine oxidasemonooxygenase LLOXMOG from Pseudomonas sp AIU 813 catalyzes the mixed bioconversion of Lamino acids particularly Llysine yielding an amide and carbon dioxide by an oxidative decarboxylation ie apparent monooxygenation as well as oxidative deamination hydrolysis of oxidized product resulting in αketo acid hydrogen peroxide H2O2 and ammonia Here using highresolution MS and monitoring transient reaction kinetics with stoppedflow spectrophotometry we identified the products from the reactions of Llysine and Lornithine indicating that besides decarboxylating imino acids ie 5aminopentanamide from Llysine LLOXMOG also decarboxylates keto acids 5aminopentanoic acid from Llysine and 4aminobutanoic acid from Lornithine The reaction of reduced enzyme and oxygen yielding an imino acid and H2O2 with no detectable C4ahydroperoxyflavin Single turnover reactions in which LLOXMOG was first reduced by Llysine to form imino acid before mixing with various compounds revealed that under anaerobic conditions only hydrolysis products are present