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Studies of the chemical basis of the origin of protein synthesis Initiation and direction of peptide growthThe data presented in this paper show that the ease of nonenzymatic activation of carboxylic acids by ATP at pH 5 varies directly with the pKa of the carboxyl group, and is consistent with the idea that it is the protonated form of the carboxyl group which participates in the activation reaction. Consequently, since most N-blocked amino acids have higher pKas than do their unblocked forms, they are activated more readily, and it has been demonstrated that this principle applies to peptides as well, which are activated more rapidly than single amino acids. It is proposed that this fact may be partly responsible for the origin of two important features still observed in contemporary protein synthesis: (1) initiation in prokaryotes is accomplished with an N-blocked amino acid, and (2) elongation in all living systems occurs at the carboxyl end of the growing peptide.
Document ID
19800065702
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Mullins, D. W., Jr.
(Alabama Univ. Birmingham, AL, United States)
Lacey, J. C., Jr.
(Alabama, University Birmingham, Ala., United States)
Date Acquired
August 10, 2013
Publication Date
August 1, 1980
Publication Information
Publication: Journal of Molecular Evolution
Volume: 15
Subject Category
Life Sciences (General)
Accession Number
80A49872
Funding Number(s)
CONTRACT_GRANT: NGR-01-010-001
Distribution Limits
Public
Copyright
Other

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