Correlation of DNA exonic regions with protein structural units in haemoglobin
- 30 April 1981
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 291 (5810) , 90-92
- https://doi.org/10.1038/291090a0
Abstract
In Hb, which has no obvious domain structure, no clear conformational characteristics have so far been recognized for the segments encoded by exons. From a close inspection of their conformations by drawing various stereodiagrams and the C.alpha.-C.alpha. distance map, a conformational characterization of the segments as structural units is proposed, using the mouse model.This publication has 20 references indexed in Scilit:
- Characterization of globin domains: Heme binding to the central exon productProceedings of the National Academy of Sciences, 1980
- The evolution and sequence comparison of two recently diverged mouse chromosomal β-globin genesCell, 1979
- The complete sequence of a chromosomal mouse α-globin gene reveals elements conserved throughout vertebrate evolutionCell, 1979
- Domains and the hinge region of an immunoglobulin heavy chain are encoded in separate DNA segmentsNature, 1979
- Comparison of cloned mouse alpha- and beta-globin genes: conservation of intervening sequence locations and extragenic homology.Proceedings of the National Academy of Sciences, 1978
- The sequence of the chromosomal mouse β-globin major gene: Homologies in capping, splicing and poly(A) sitesCell, 1978
- Do genes-in-pieces imply proteins-in-pieces?Nature, 1978
- Sequence of a mouse germ-line gene for a variable region of an immunoglobulin light chain.Proceedings of the National Academy of Sciences, 1978
- Why genes in pieces?Nature, 1978
- Tertiary Structure of Proteins. I. Representation and Computation of the ConformationsJournal of the Physics Society Japan, 1972