Ship

A ship is a large buoyant watercraft. Ships are generally distinguished from boats based on size, shape and cargo or passenger capacity. Ships are used on lakes, seas,rivers,and oceans for a variety of activities, such as the transport of people or goods, fishing, entertainment, public safety, and warfare. Historically, a "ship" was a sailing vessel with at least three square-rigged masts and a full bowsprit.

In armed conflict and in daily life, ships have become an integral part of modern commercial and military systems. Fishing boats are used by millions of fishermen throughout the world. Military forces operate vessels for naval warfare and to transport and support forces ashore. Commercial vessels, nearly 35,000 in number, carried 7.4 billion tons of cargo in 2007. As of 2011, there are about 104,304 ships with IMO numbers in the world.

Ships were always a key in history's great explorations and scientific and technological development. Navigators such as Zheng He spread such inventions as the compass and gunpowder. Ships have been used for such purposes as colonization and the slave trade, and have served scientific, cultural, and humanitarian needs. After the 16th century, new crops that had come from and to the Americas via the European seafarers significantly contributed to the world population growth.Ship transport has shaped the world's economy into today's energy-intensive pattern.

Ship (disambiguation)

A ship is a large vessel that floats on water, specifically the ocean and the sea.

Ship or ships may also refer to:

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Ship (comics)

The fictional A.I. entity originally known as Ship has appeared in several incarnations in the Marvel Universe. At times controlled by both the X-Men and their enemies, the sentient A.I. has at times been installed in the core of a Celestial starship, two space stations, and a techno-organic being. It is not related to Star-Lord's "Ship".

Fictional character biography

Ancient history

Ship's A.I. was created untold millennia ago by the Celestials as the operating system for a data collection device. The Celestials had genetically manipulated humanity, and they left the Ship in the area that would come to be known as Mongolia to monitor humanity's progress.

Circa 1100 A.D., a Mongolian immortal known as Garbha-Hsien (later known as Saul), discovered the Ship and lived next to it while he researched its mysteries. Saul never attempted to enter the Ship.

In time, the Egyptian immortal En Sabah Nur learned of Saul and sought him out as another immortal. In a confrontation, En Sabah Nur slew all of Saul's guards. Saul then sought to humble his fellow "forever-walker" by revealing the secret titanic vessel. Having had previous experience with futuristic technology due to his encounters with Rama-Tut, Nur attacked Saul and left the other immortal for dead and entered the Ship. He emerged later as a vastly changed being who now called himself Apocalypse.

TPM

TPM may refer to:

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Other uses

Tropomyosin 3

Tropomyosin alpha-3 chain is a protein that in humans is encoded by the TPM3 gene.

This gene encodes a member of the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins that polymerize end-to-end along the major groove in most actin filaments. They provide stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, they regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in this gene result in autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are associated with cancer. Multiple transcript variants encoding different isoforms have been found for this gene.

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TPM2

β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.

Structure

β-tropomyosin is roughly 32 kDa in molecular weight (284 amino acids), but multiple splice variants exist. Tropomysin is a flexible protein homodimer or heterodimer composed of two alpha-helical chains, which adopt a bent coiled coil conformation to wrap around the seven actin molecules in a functional unit of muscle. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. Tropomyosin dimers are composed of varying combinations of tropomyosin isoforms; human striated muscles express protein from the TPM1 (α-tropoomyosin), TPM2 (β-tropomyosin) and TPM3 (γ-tropomyosin) genes, with α-tropomyosin being the predominant isoform in striated muscle. Fast skeletal muscle and cardiac muscle contain more αα-homodimers, and slow skeletal muscle contains more ββ-homodimers. In human cardiac muscle the ratio of α-tropomyosin to β-tropomyosin is roughly 5:1. It has been shown that different combinations of tropomyosin isoforms bind troponin T with differing affinities, demonstrating that isoform combinations are used to impart a specific functional impact.