Biomedical subjects

H J Stirk

Publications and source records attributed to H J Stirk.

5 recordsLinked to original sources

PubMed1995

Long loops in proteins.

In proteins, loop regions which connect secondary structures are generally short (80% are <10 amino acids long). However, long loops, defined here as > or = 10 residues, do occur. Two types of long loop may be distinguished: those which connect adjacent regions of secondary structure ('long-closed') and those which connect distant secondary structures ('long-open'). Only 5% of all loops in proteins fall into the long-open class. Inspection of these unusual long-open loops reveals a higher percentage of proline residues and more helix-helix linkages than expected. Exposure to solvent is similar for long-open and long-closed loops. The role of these loops in protein folding is discussed.

Amino Acid Sequence↗

PubMed1994

The BC loop in poliovirus coat protein VP1: an ideal acceptor site for major insertions.

In poliovirus the BC loop of the VP1 coat protein is hypervariable and can accommodate numerous foreign sequences introduced by genetic engineering. This paper examines the characteristics of the VP1 BC loop of the picornaviruses to see why this loop is so variable and particularly favourable for the insertion of foreign sequences leading to the formation of chimeric particles. The characteristics which make this loop distinctive can be used to find equally permissive loops in other proteins.

Amino Acid Sequence↗

PubMed1992

Depicting topology and handedness in jellyroll structures.

The jellyroll structure is a special case of the Greek key topology and, to date, has only been observed in complete form in one of its four possible arrangements. Like other elements of super-secondary structure involving the beta-strand (e.g. the beta alpha beta unit) the known structure forms a right-handed superhelix. The possibility of losing such tertiary information and other problems associated with representing these structures by two-dimensional topology diagrams are discussed. A series of rules are presented which allow this three-dimensional information to be represented in two-dimensional topology diagrams from which the handedness of a jellyroll structure can be determined.

Protein Conformation↗

PubMed1992

A topological model for hepatitis B surface antigen.

A model of hepatitis B surface antigen has been derived, based on extensive sequence analysis and biochemical data. The surface antigen sequences of the human, woodchuck, ground squirrel and duck hepadnaviruses were examined using hydrophobicity, hydrophobic moments, flexibility and secondary structure prediction. The helix phase diagram, which is a modified version of Eisenberg's hydrophobic moment plots and which specifically addresses the problem of transmembrane helices, was used to examine the predicted helices. In this model four transmembrane helices are predicted. The N and C termini and the second hydrophilic region, which bears the major B-cell antigenic determinants, are external. It is suggested that the transmembrane helices may pack to form a channel through the membrane and may also be involved in the mechanisms of cell entry. A significant difference between the duck hepadnavirus and the mammalian HBsAg sequences was found, hence care must be taken when extrapolating data between the duck and the human surface antigen.

Amino Acid Sequence↗

PubMed1985

Enzyme studies in biotin-responsive disorders.

There appear to be at least two underlying aetiologies for combined carboxylase deficiency; firstly, a failure of biotinylation of apocarboxylases due to a mutation of holocarboxylase synthetase (EC 6.3.4.10) which results in an enzyme with a high Km with respect to biotin and secondly, a failure of biotinylation due to a lowered availability of biotin due to biotinidase deficiency (EC 3.5.1.12). In both these disorders secondary defects of all four biotin-dependent carboxylases result which in turn causes the excretion of the metabolites characteristic of the isolated carboxylase deficiencies. In addition, both disorders respond biochemically and clinically to the administration of large amounts of biotin.

Acetyl-CoA Carboxylase↗