Olha o flagelo bacteriano aí, gente!

O atual “konsensus” acadêmico afirma que o Design Inteligente é pseudociência, não propõe predições, não pode ser falsificado, é falsa ciência, “criacionismo disfarçado em smoking barato”, não publica artigos em publicações científicas com revisão por pares [Como, se a nós teóricos e proponentes da TDI é vedado publicar, e nem se defender nesses periódicos???] y otras cositas mais.

Contudo, há muito tempo que as teses de complexidade irredutível e informação complexa especificada vêm tirando o sono da KGB da Nomenklatura científica, e já está contribuindo para a revisão do neodarwinismo (Darwin 3.0 em 2010).

A galera dos meninos e meninas de Darwin então é useira e vezeira em afirmar na internet que as teses de Behe foram falsificadas e que a Akademia já tem como explicar a complexidade irredutível dos sistemas bióticos através de processos gradualistas darwinianos. Nada mais falso!

NOTA BENE: NADA MAIS FALSO! A tese de Behe, o flagelo bacteriano, permanece não falsificada pela Nomenklatura científica, e até poderia virar samba enredo do Salgueiro no carnaval de 2008: “Olha o flagelo bacteriano aí, gente!!!”

Prova disso é que alguns cientistas mais sérios e que estão lidando com esta questão, vão abordar, o que mesmo que vão abordar??? O flagelo bacteriano!!! A teoria da evolução de Darwin não explica a origem e evolução de uma “simples” bactéria, poderia explicar toda a complexidade e diversidade de vida? É pensar cum granum salis sobre isso, e considerar outras opções teóricas...

Vide abaixo, em inglês, sorry periferia (obrigado, Ibrahim Sued): 100% Design Inteligente!!!

NOTA DE ESCLARECIMENTO: Nenhum desses cientistas propõe o Design Inteligente e, até onde eu sei, são todos darwinistas.

Single Molecules and Molecular Machines

Sponsored by:

California Institute for Quantitative Biosciences and The New York Academy of Sciences


Organizers:

Clayton Heathcock and Susan Marqusee, California Institute for Quantitative Biosciences (QB3)

Advances in single molecule methods have resulted in the exciting, burgeoning field of single molecule biophysics. These approaches have been exceptionally important in studies on molecular motors, the biological machines essential for providing force and movement in living organisms. Leaders in the field will present studies that reveal new behaviors and molecular details that are obscured by traditional ensemble-based approaches.

The California Institute for Quantitative Biosciences (QB3) is a partnership between the state of California, the University of California campuses at Berkeley, San Francisco, and Santa Cruz, and private industry and venture capital. Armed with the quantitative tools integral to physics, chemistry, engineering, and mathematics, QB3's 170 researchers decipher the complex systems involved in living systems and discover ground-breaking applications for that basic knowledge in the areas of health, energy, and the environment.

Please note that QB3 faculty affiliates may attend for free and must register through email nymeetings@nyas.org .

Order of Talks

Welcoming Remarks
Professor Susan Marqusee, QB3
Jeremy Paul, The New York Academy of Sciences

Morning Session
James Spudich, Stanford University
Arne Gennerich, University of California, San Francisco

Coffee Break, Atrium Lobby
Carlos Bustamante, University of California, Berkeley
TBD

Lunch, Atrium Lobby

Afternoon Session
George Oster, University of California, Berkeley
Jan Liphardt, University of California, Berkeley

Coffee Break, Atrium Lobby
Jeff Moffitt, University of California, Berkeley
Howard Berg, Harvard University

Abstracts

Tension Sensing and the Remarkable Myosin Motor
James Spudich
Stanford University
The molecular basis of how myosin motors work has been significantly advanced by studies of myosins V and VI. Myosin V moves processively by stepping arm-over-arm, walking along the 36-nm pseudo-repeat of an actin filament by swinging its long lever arms through an angle of ~70o, and hydrolyzing one ATP per step. Intramolecular tension sensing establishes a bias in the behavior of the two heads with regard to nucleotide kinetics that allows the rear head to most often release from the actin by binding ATP. Recently, we have improved time resolution to submilliseconds by tracking single gold nanoparticle-myosin V conjugates using darkfield imaging, and have directly observed the behavior of the unbound head as the motor translocates. We have also developed a technique called single-molecule high resolution co-localization (SHREC), which allows simultaneous co-localization of two chromatically differing fluorophores only 10 nm apart. We used SHREC to directly observe myosin V molecules walking hand-over-hand. We are now adapting SHREC to observe myosin V's nucleotide dynamics using dye-labeled ATP molecules. Myosin VI has been the biggest challenge to the lever arm hypothesis of myosin movement. It has a very short lever arm that is only two light chains long. Nevertheless, the molecule surprisingly steps processively 36 nm along an actin filament. Furthermore, myosin VI moves in the opposite direction to that of myosin II and myosin V. Our most recent work shows how this unusual motor achieves these feats. Myosin VI is now a paradigm of how intermolecular tension sensing is translated into biologically important trafficking regulation.
Coathors: Alex Dunn, Stirling Churchman, Zev Bryant, David Altman

Force-Induced Bidirectional Stepping of Cytoplasmic Dynein
Arne Gennerich
University of California, San Francisco

Following Translation by Single Ribosomes One Codon at a Time
Carlos Bustamante
University of California, Berkeley
I will present our newest results on exploring the dynamics of translation using optical tweezers to follow the real-time movement of single ribosomes along single messenger RNAs. The messenger RNAs were designed to form either a 60-bp or a 274-bp hairpin. The RNA was held at a force below its unfolding transition, and translation was followed by the increase in end-to-end distance as the hairpin was unwound by the translating ribosome. Translation occurs by a series of successive translocation-and-pause steps. The distribution of pause durations, with a median value of 2.8 s, indicates that at least two rate-determining processes control the pause. Each translocation step measured three bases - one codon - and occurred in less than 0.1 s. Analysis of the times required for translocation reveals that there are three substeps in the process. Increasing force applied to the ends of the RNA hairpin destabilized secondary structures and decreased pause durations, but did not affect translocation times. Thus, translocation occurs with a constant and rapid velocity strictly coupled and coordinated to the unwinding of base pairs at the entrance to the ribosome. The presence of internal Shine-Dalgarno-like sequences in the messenger RNA tended to cause translation arrest. I will discuss also some of the current and future directions for this project.
Coauthors: Jin-Der Wen, Laura Lancaster, Courtney Dodges, Harry Noller, Ignacio Tinoco Jr.

How the World's Smallest Rotary Motor Works
George Oster
University of Califronia, Berkeley
ATP synthase (also called FoF1 ATPase) is the universal enzyme that manufactures ATP from ADP and phosphate using the energy derived from a transmembrane protonmotive gradient. It can also reverse itself and hydrolyze ATP to pump protons against an electrochemical gradient. This protein consists of two rotary motors connected to a common shaft, and rotating in the opposite direction. The F1 motor generates a mechanical torque using the hydrolysis energy of ATP. The Fo motor generates a rotary torque in the opposite direction using the energy stored in a transmembrane electrochemical gradient. Thus ATP synthase comprises what must be the world's smallest rotary engine. Each motor can be reversed: The Fo motor can drive the F1 motor in reverse to synthesize ATP, and the F1 motor can drive the Fo motor in reverse to pump protons. Thus ATP synthase exhibits two of the major energy transduction pathways employed by the cell to convert chemical energy into mechanical force. I will present a model for this molecular machine that accounts for all of the experimentally measured mechanochemical behavior.

Viral DNA Packaging: One Base Pair at a Time
Jeff Moffitt
University of California, Berkeley

Flights of the Flagellar Rotary Motor
Howard Berg
Harvard University
Flagellated bacteria swim by rotating long, thin, helical filaments that arise at different points on the cell surface. Each filament is driven at its base by a rotary motor only 45 nm in diameter made from about 20 different kinds of parts. Control of the direction of rotation of such motors is the basis for the chemotactic response, i.e., for the ability of cells to swim up spatial gradients of chemical attractants. I will review what is known about the flagellar motor and describe its behavior near the limit of zero external load.

New Tools for Characterizing Single Biomolecules: Plasmon Rulers and Nanopores
Jan Liphardt
University of California, Berkeley

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