Editorial: hypotheses about protein folding - the proteomic code and wonderfolds
Author:
Publisher
Springer Science and Business Media LLC
Subject
Health Informatics,Modelling and Simulation
Link
http://link.springer.com/content/pdf/10.1186/1742-4682-6-31.pdf
Reference14 articles.
1. Preuss M, Miller AD: The affinity of the GroEL/GroES complex for peptides under conditions of protein folding. FEBS Lett. 2000, 466: 75-79. 10.1016/S0014-5793(99)01748-2.
2. Pintar A, Pongor S: The "first in-last out" hypothesis on protein folding revisited. Proteins. 2005, 60: 584-590. 10.1002/prot.20529.
3. Biró JC: Indications that "codon boundaries" are physico-chemically defined and that protein-folding information is contained in the redundant exon bases. Theor Biol Med Model. 3: 28-10.1186/1742-4682-3-28.
4. Biró JC: Protein folding information in nucleic acids which is not present in the genetic code. Ann N Y Acad Sci. 2006, 1091: 399-411. 10.1196/annals.1378.083.
5. Biró JC: The Proteomic Code: a molecular recognition code for proteins. Theor Biol Med Model. 4: 45-10.1186/1742-4682-4-45.
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