Determination for the modal age level for the grades IV and VI of the difficulty of the principle: "The amount of momentum possessed by an object depends upon its weight and speed of motion.

Thesis (M.A.)--Boston Universit

Concert recording 2018-11-03

[Track 1]. Broodin\u27 / Asher Perkins -- [Track 2]. Mary had a little lamb / Buddy Guy arranger Stevie Ray Vaughan -- [Track 3]. Little wing / Jimi Hendrix arranger Stevie Ray Vaughan -- [Track 4]. Scuttlebuttin / Stevie Ray Vaughan -- [Track 5]. Sirabhorn / Pat Metheny -- [Track 6]. Outerstellar mozy [Track 7]. Truth? [Track 8]. Street swing [Track 9]. Warm kages / Asher Perkins -- [Track 10]. The saga of Harrison Crabfeathers / Steve Kuhn

Statics and dynamics of single DNA molecules confined in nanochannels

The successful design of nanofluidic devices for the manipulation of biopolymers requires an understanding of how the predictions of soft condensed matter physics scale with device dimensions. Here we present measurements of DNA extended in nanochannels and show that below a critical width roughly twice the persistence length there is a crossover in the polymer physics

Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g

Crista junctions (CJs) are important for mitochondrial organization and function, but the molecular basis of their formation and architecture is obscure. We have identified and characterized a mitochondrial membrane protein in yeast, Fcj1 (formation of CJ protein 1), which is specifically enriched in CJs. Cells lacking Fcj1 lack CJs, exhibit concentric stacks of inner membrane in the mitochondrial matrix, and show increased levels of F1FO–ATP synthase (F1FO) supercomplexes. Overexpression of Fcj1 leads to increased CJ formation, branching of cristae, enlargement of CJ diameter, and reduced levels of F1FO supercomplexes. Impairment of F1FO oligomer formation by deletion of its subunits e/g (Su e/g) causes CJ diameter enlargement and reduction of cristae tip numbers and promotes cristae branching. Fcj1 and Su e/g genetically interact. We propose a model in which the antagonism between Fcj1 and Su e/g locally modulates the F1FO oligomeric state, thereby controlling membrane curvature of cristae to generate CJs and cristae tips

Enhancement of the in vivo circulation lifetime of l-α-distearoylphosphatidylcholine liposomes: importance of liposomal aggregation versus complement opsonization

AbstractIncorporation of N-(ω-carboxy)acylamido-phosphatidylethanolamines (-PEs) into large unilamellar vesicles (LUVs) of l-α-distearoylphosphatidylcholine (DSPC) was found to dramatically increase the in vivo liposomal circulation lifetime in rats, reaching a maximal effect at 10 mol.% of the total phospholipid. Neither pure DSPC liposomes nor those with the longest circulating derivative, N-glutaryl-dipalmitoylphosphatidylethanolamine (-DPPE), were found to significantly bind complement from serum. Therefore, the relatively short circulation time of pure DSPC liposomes did not appear to be related to greater complement opsonization leading to uptake by the reticuloendothelial system. However, N-(ω-carboxy)acylamido-PEs were particularly efficient inhibitors of a limited aggregation detected for pure DSPC liposomes. The aggregation tendency of DSPC liposomes incorporating various structural analogs of N-glutaryl-DPPE correlated inversely with the circulation lifetimes. Therefore, it is concluded that such PE derivatives enhance the circulation time by preventing liposomal aggregation and avoiding a poorly understood mechanism of clearance that is dependent on size but is independent of complement opsonization. At high concentrations of N-glutaryl-DPPE (above 10 mol.%), the liposomes exhibited strong complement opsonization and were cleared from circulation rapidly, as were other highly negatively charged liposomes. These data demonstrate that both the lack of opsonization and the lack of a tendency to aggregate are required for long circulation. Liposomal disaggregation via N-(ω-carboxy)acylamido-PEs yields a new class of large unilamellar DSPC liposomes with circulation lifetimes that are comparable to those of sterically stabilized liposomes

Under the microscope: Single molecule symposium at the University of Michigan, 2006

In recent years, a revolution has occurred in the basic sciences, which exploits novel single molecule detection and manipulation tools to track and analyze biopolymers in unprecedented detail. A recent Gordon Research Conference style meeting, hosted by the University of Michigan, highlighted current status and future perspectives of this rising field as researchers begin to integrate it with mainstream biology and nanotechnology. © 2006 Wiley Periodicals, Inc. Biopolymers 85:106–114, 2007Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/55865/1/20621_ftp.pd

Concert recording 2018-04-19b

[Track 1]. Sonatina meridional / Manuel Ponce -- [Track 2]. Etude no. 6 / Hector Villa-Lobos -- [Track 3]. Milonga / Jorge Cardoso -- [Track 4]. Straight no chaser / T. Monk -- [Track 5]. A child is born / T. Monk -- [Track 6]. Autumn leaves / J. Kosma -- [Track 7]. Body and soul / J. Green -- [Track 8]. All the things you are / J. Kern -- [Track 9]. 4 on 6 / Wes Montgomery -- [Track 10]. Bright size life / P. Metheny -- [Track 11]. Dueling banjos / Arthur Smith -- [Track 12]. Elenor Rigby / Lennon and McCartney -- [Track 13]. Alone / Bryce Holcomb -- [Track 14]. All around me / Flyleaf -- Vital transformation / Mahavisunu Orchestra

A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria

Peer reviewedPublisher PD

Human PrimPol is a highly error-prone polymerase regulated by single-stranded DNA binding proteins

PrimPol is a recently identified polymerase involved in eukaryotic DNA damage tolerance, employed in both re-priming and translesion synthesis mechanisms to bypass nuclear and mitochondrial DNA lesions. In this report, we investigate how the enzymatic activities of human PrimPol are regulated. We show that, unlike other TLS polymerases, PrimPol is not stimulated by PCNA and does not interact with it in vivo. We identify that PrimPol interacts with both of the major single-strand binding proteins, RPA and mtSSB in vivo. Using NMR spectroscopy, we characterize the domains responsible for the PrimPol-RPA interaction, revealing that PrimPol binds directly to the N-terminal domain of RPA70. In contrast to the established role of SSBs in stimulating replicative polymerases, we find that SSBs significantly limit the primase and polymerase activities of PrimPol. To identify the requirement for this regulation, we employed two forward mutation assays to characterize PrimPol's replication fidelity. We find that PrimPol is a mutagenic polymerase, with a unique error specificity that is highly biased towards insertion-deletion errors. Given the error-prone disposition of PrimPol, we propose a mechanism whereby SSBs greatly restrict the contribution of this enzyme to DNA replication at stalled forks, thus reducing the mutagenic potential of PrimPol during genome replication