Almost 10 years ago, a study was published which examined the amino acid pairs represented by particular triplet codons and their complementary sequences (anti-sense codons) (Biro, 1981). These complementary amino acid pairs displayed 'hydropathic anti-complementarity' in that hydrophobic residues almost always were partnered with hydrophilic amino acids, whereas amphiphilic residues tended to be paired with other amphiphilic amino acids (Blalock & Smith, 1984). These reports remained no more than interesting observations on the nature of the genetic code until the remarkable finding that the peptides adrenocorticotrophin(1–24) (ACTH(1–24)) and γ-endorphin (a 17-mer) bound specifically and with a relatively high degree of affinity (∼10−6 mol/l) to their respective complementary peptides (CP)—molecules synthezised using a template RNA complementary to the original mRNA for the peptides, translation being in a 5′→3′ direction and in the same reading frame (Bost, Smith & Blalock, 1985a). In the intervening years, evidence for the binding
Journal of Endocrinology is committed to supporting researchers in demonstrating the impact of their articles published in the journal.
The two types of article metrics we measure are (i) more traditional full-text views and pdf downloads, and (ii) Altmetric data, which shows the wider impact of articles in a range of non-traditional sources, such as social media.
More information is on the Reasons to publish page.
| Sept 2018 onwards | Past Year | Past 30 Days | |
|---|---|---|---|
| Full Text Views | 0 | 0 | 0 |
| PDF Downloads | 0 | 0 | 0 |
Online ISSN: 1479-6805
Print ISSN: 0022-0795
Strengthening biomedical communities
to advance science and health
CONTACT US
Bioscientifica Ltd | Starling House | 1600 Bristol Parkway North | Bristol BS34 8YU | UK
Bioscientifica Ltd | Registered in England no 3190519
