Dragon's Domain

"Dragon's Domain" is the twenty-third episode of the first series of Space: 1999. The screenplay was written by Christopher Penfold; the director was Charles Crichton. The final shooting script was dated 21 January 1975, with blue-page amendments dated 29 January 1975 and yellow-page amendments dated 30 January 1975. Live-action filming took place Monday 27 January 1975 through Monday 10 February 1975.

Story

It is 877 days after leaving Earth orbit, and the Moon is passing through a stretch of peaceful empty space between galaxies. Doctor Helena Russell is alone in her quarters, typing a report on a World Space Commission Medical Department form regarding the status of astronaut Captain Tony Cellini. Hours earlier, during the simulated 'night-time' on Moonbase Alpha, Cellini awakens in a cold sweat. Sensing danger, he seizes an antique tomahawk from a decorative weapons display. After making several lunges at an imagined enemy (which he perceives as a swirling display of light accompanied by an electronic screeching sound), Cellini ends up hacking the tomahawk deep into the communications post in his quarters.

Laplace transform

In mathematics the Laplace transform is an integral transform named after its discoverer Pierre-Simon Laplace (/ləˈplɑːs/). It takes a function of a positive real variable t (often time) to a function of a complex variable s (frequency).

The Laplace transform is very similar to the Fourier transform. While the Fourier transform of a function is a complex function of a real variable (frequency), the Laplace transform of a function is a complex function of a complex variable. Laplace transforms are usually restricted to functions of t with t > 0. A consequence of this restriction is that the Laplace transform of a function is a holomorphic function of the variable s. So unlike the Fourier transform, the Laplace transform of a distribution is generally a well-behaved function. Also techniques of complex variables can be used directly to study Laplace transforms. As a holomorphic function, the Laplace transform has a power series representation. This power series expresses a function as a linear superposition of moments of the function. This perspective has applications in probability theory.

S1 domain

The S1 domain is a protein domain that was originally identified in ribosomal protein S1 but is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding domain from the Escherichia coli polynucleotide phosphorylase has been determined using NMR methods and consists of a five-stranded antiparallel beta barrel. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site.

The structure of the S1 domain is very similar to that of cold shock proteins. This suggests that they may both be derived from an ancient nucleic acid-binding protein.

References

This article incorporates text from the public domain Pfam and InterPro IPR003029

S4 protein domain

In molecular biology, S4 domain refers to a small protein domain found in a large ribosomal protein named S4. The S4 domain is a small domain, approximately 60-65 amino acid residues long, occurs in a single copy at various positions in different proteins and was originally found in pseudouridine synthases, a bacterial ribosomal protein. The function of the ribosome is to read RNA and synthesise the correct protein. The S4 domain functions in RNA binding. By improving RNA binding it aids the process of protein synthesis and leads to fewer errors. Since the S4 domain is a ribosomal protein, this function is fundamental to protein synthesis.

Proteins S4 helps initiate assembly of the 16S rRNA, are located at junctions of five RNA helices. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome.