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J C Shepherd

Publications and source records attributed to J C Shepherd.

26 records · Page 2Linked to original sources
PubMed1981

Method to determine the reading frame of a protein from the purine/pyrimidine genome sequence and its possible evolutionary justification.

The periodic variations obtained by correlating the relative positions of purines and pyrimidines (and of the four bases thymine, cytosine, adenine, and guanine) in a wide variety of genomes of wholly or partly known sequence suggest that there may be enough of an earlier comma-free coding system (i.e., only readable in one frame) still present to permit determination of the reading frame and approximate extent of the present protein coding stretches. The characteristics of these variations support the hypothesis that these primitive messages were formed of coding triplets having the form RNY (R = purine; Y = pyrimidine; and N = purine or pyrimidine). The base sequences and reading frames that have a minimal deviation from such a message are still good predictors of actual coding regions and reading frames in spite of the many mutations that have occurred since such a genetic code was last in use. In fact, the right frame for almost all the proteins in a number of viruses and various prokaryotes and eukaryotes is deduced purely from purine/pyrimidine information and not by using the normal start and stop signals.

Biological Evolution↗
PubMed1979

The influence of cholesterol on head group mobility in phospholipid membranes.

The dielectric dispersion in the MHz range of the zwitterionic dipolar phosphocholine head groups has been measured from 0--70 degrees C for various mixtures of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and cholesterol. The abrupt change in the derived relaxation frequency f2 observed for pure DPPC at the gel-to-liquid crystalline phase transition at 42 degrees C reduces to a more gradual increase of frequency with temperature as the cholesterol content is increased. In general the presence of cholesterol increases the DPPC head group mobility due to its spacing effect. Below 42 degrees C no sudden changes in f2 are found at 20 or 33 mol% cholesterol, where phase boundaries have been suggested from other methods. Above 42 degrees C, however, a decrease in f2 at cholesterol contents up to 20--30 mol% is found. This is thought to be partly due to an additional restricting effect of the cholesterol on the number of hydrocarbon chain conformations and consequently on the area occupied by the DPPC molecules.

Cholesterol↗
PubMed1978

Zwitterionic dipoles as a dielectric probe for investigating head group mobility in phospholipid membranes.

For phospholipid membranes with zwitterionic head groups, the dipole can be considered as a specific label for tracing the changes in the dynamic behaviour of this region of the bilayer in its various phases. Measurements of the dielectric properties of fully hydrated 1,2-dipalmitoyl-sn-glycero-3-phosphocholine bilayers in the frequency range 1--50 MHz show a dispersion which is attributed to the motion of the phosphocholine dipoles in the plane of the bilayers. When the temperature is varied, both the permittivity and loss factor increase sharply at the pretransition (35 degrees C) and the main transition (42 degress C). The relaxation time and amplitude were also determined for this dispersion and these further reflect the structural changes occurring with temperature. The relaxation times varied between 4 ns at 30 degrees C and 2.3 ns at 50 degrees C. Due to steric hindrances a restriction in the angle of head group rotation occurs at lower temperatures but is greatly reduced above the main transition.

Ions↗
PubMed1977

Dielectric dispersion of DL-alpha-valine in aqueous solution.

The complex permittivity (epsilon = epsilon - jepsilon) of an (0.5 M) aqueous solution of DL-alpha-valine was measured at microwave frequencies over the temperature range 0.3 - 40 degrees C. The magnitude and relaxation time of the dispersions were determined, and the results interpreted in terms of the molecular structure of the valine molecule in solution. The peak in the dielectric loss due to the relaxation of the valine molecules occurs at approximately 2.6 GHz at 37 degrees C.

Electric Conductivity↗
PubMedDate not supplied

Fly and frog homoeo domains show homologies with yeast mating type regulatory proteins.

Homoeotic genes in the bithorax and Antennapedia complexes of Drosophila melanogaster appear to specify the developmental fate of segments of the fly. Some of these genes (Ultrabithorax, Antennapedia and fushi tarazu) share homology due to their conservation of a 'homoeo domain'1,2 consisting of 60 amino acids. Cross-hybridization and cloning experiments show that the homoeo domain is conserved in a frog (Xenopus laevis) gene expressed in early development and may also be present in earthworm, beetle, chicken, mouse and human genomes. The extreme conservation found in the amino acid sequences between the Drosophila and Xenopus domains suggests that the domain has a vital function in the control of early development. Here we report the results of a search made in the Dayhoff sequence bank, which reveals a lesser but apparently significant homology between the homoeo domain and the amino acids coded from parts of the a 1 and alpha 2 mating type genes of the yeast Saccharomyces cerevisiae.

Amino Acid Sequence↗
PubMedDate not supplied

A hybrid recognition sequence in a recombinant restriction enzyme and the evolution of DNA sequence specificity.

Early attempts to generate new restriction specificities by recombination between allelic restriction-modification systems have been unsuccessful. Bullas et al. succeeded in isolating a new specificity, SQ, in Salmonella that they interpreted as being the result of a recombination event between the parental strains, Salmonella typhimurium and S. postdam, which encode the SB and SP restriction systems, respectively. This interpretation has recently been confirmed by DNA heteroduplex studies with the SB, SP and SQ structural genes. We have determined the DNA sequences recognized by the SB and SP enzymes and found that, like all type I restriction sequences, they are split into two specific domains by a spacer of nonspecific sequence that, for both SB and SP, is 6 base pairs (bp) long. We have now determined the sequence recognized by the recombinant SQ enzyme and find that it is a hybrid between the SB and SP sequences, containing one specific domain from each parental strain. This result implies that each of the two specific domains is recognized by a physically distinct part of the enzyme.

Alleles↗