Match!
Charles W. Carter
University of North Carolina at Chapel Hill
ChemistryBiochemistryStereochemistryCrystallographyBiology
143Publications
36H-index
5,789Citations
What is this?
Publications 138
Newest
#1Charles W. Carter (UNC: University of North Carolina at Chapel Hill)H-Index: 36
Conversion of the free energy of NTP hydrolysis efficiently into mechanical work and/or information by transducing enzymes sustains living systems far from equilibrium, and so has been of interest for many decades. Detailed molecular mechanisms, however, remain puzzling and incomplete. We previously reported that catalysis of tryptophan activation by tryptophanyl-tRNA synthetase, TrpRS, requires relative domain motion to re-position the catalytic Mg(2+) ion, noting the analogy between that condi...
2 CitationsSource
#1Charles W. Carter (UNC: University of North Carolina at Chapel Hill)H-Index: 36
#2Alex Popinga (University of Auckland)H-Index: 4
Last. Peter R. Wills (University of Auckland)H-Index: 23
view all 4 authors...
Phylogenetic arguments that the adaptive radiation of the Class I aminoacyl-tRNA synthetases, aaRS, occurred after the genetic code had been extensively stabilized conflict with recent experimental data showing that ancestors of the two aaRS Classes arose on opposite strands of a single gene. The latter result necessarily implies that phylogenies for both Classes trace from a time when genetic coding used protein aaRS restricted to a far simpler amino acid alphabet. This conundrum resolves if tr...
Source
#1Charles W. Carter (UNC: University of North Carolina at Chapel Hill)H-Index: 1
#2Peter R. Wills (University of Auckland)H-Index: 23
Abstract How genetic coding differentiated biology from chemistry is a long-standing challenge in Biology, for which there have been few experimental approaches, despite a wide-ranging speculative literature. We summarize five coordinated areas—experimental characterization of functional approximations to the minimal peptides (protozymes and urzymes) necessary to activate amino acids and acylate tRNA; showing that specificities of these experimental models match those expected from the synthetas...
2 CitationsSource
Source
#1Charles W. Carter (UNC: University of North Carolina at Chapel Hill)H-Index: 36
#2Peter R. Wills (University of Auckland)H-Index: 23
: The genetic code likely arose when a bidirectional gene replicating as a quasi-species began to produce ancestral aminoacyl-tRNA synthetases (aaRS) capable of distinguishing between two distinct sets of amino acids. The synthetase class division therefore necessarily implies a mechanism by which the two ancestral synthetases could also discriminate between two different kinds of tRNA substrates. We used regression methods to uncover the possible patterns of base sequences capable of such discr...
2 CitationsSource
#1Charles W. Carter (UNC: University of North Carolina at Chapel Hill)H-Index: 36
#2Peter R. Wills (University of Auckland)H-Index: 23
ABSTRACT The genetic code likely arose when a bidirectional gene began to produce ancestral aminoacyl-tRNA synthetases (aaRS) capable of distinguishing between two distinct sets of amino acids. The synthetase Class division therefore necessarily implies a mechanism by which the two ancestral synthetases could also discriminate between two different kinds of tRNA substrates. We used regression methods to uncover the possible patterns of base sequences capable of such discrimination and find that ...
Source
#1Charles W. Carter (UNC: University of North Carolina at Chapel Hill)H-Index: 36
#2Violetta Weinreb (UNC: University of North Carolina at Chapel Hill)H-Index: 12
Last. Nikolay V. Dokholyan (PSU: Pennsylvania State University)H-Index: 60
view all 6 authors...
The D1 switch is a packing motif, broadly distributed in the proteome, that couples tryptophanyl-tRNA synthetase (TrpRS) domain movement to catalysis and specificity, thereby creating an escapement mechanism essential to free-energy transduction. The escapement mechanism arose from analysis of an extensive set of combinatorial mutations to this motif, which allowed us to relate mutant-induced changes quantitatively to both kinetic and computational parameters during catalysis. To further charact...
1 CitationsSource
#1Marc Potempa (UNC: University of North Carolina at Chapel Hill)H-Index: 6
#2Sook Kyung Lee (UNC: University of North Carolina at Chapel Hill)H-Index: 5
Last. Ronald Swanstrom (UNC: University of North Carolina at Chapel Hill)H-Index: 62
view all 9 authors...
Abstract Retroviral proteases (PRs) have a unique specificity that allows cleavage of sites with or without a P1′ proline. A P1′ proline is required at the MA/CA cleavage site due to its role in a post-cleavage conformational change in the capsid protein. However, the HIV-1 PR prefers to have large hydrophobic amino acids flanking the scissile bond, suggesting that PR recognizes two different classes of substrate sequences. We analyzed the cleavage rate of over 150 combinations of six different ...
Source
#1Charles W. Carter (UNC: University of North Carolina at Chapel Hill)H-Index: 36
#2Peter R. Wills (University of Auckland)H-Index: 23
: Class I and II aaRS recognition of opposite grooves was likely among the earliest determinants fixed in the tRNA acceptor stem bases. A new regression model identifies those determinants in bacterial tRNAs. Integral coefficients relate digital dependent to independent variables with perfect agreement between observed and calculated grooves for all twenty isoaccepting tRNAs. Recognition is mediated by the Discriminator base 73, the first base pair, and base 2 of the acceptor stem. Subsets of th...
7 CitationsSource
#1Marc Potempa (UNC: University of North Carolina at Chapel Hill)H-Index: 6
#2S.K. Lee (UNC: University of North Carolina at Chapel Hill)H-Index: 5
Last. Ronald Swanstrom (UNC: University of North Carolina at Chapel Hill)H-Index: 62
view all 9 authors...
Retroviral proteases (PR) have a unique specificity that allows cleavage of sites with or without a P1 prime proline. A P1 prime proline is required at the MA/CA cleavage site due to its role in a post-cleavage conformational change in the capsid protein. However, the HIV-1 PR prefers to have large hydrophobic amino acids flanking the scissile bond, suggesting PR recognizes two different classes of substrate sequences. We analyzed the cleavage rate of over 150 iterations of six different HIV-1 c...
Source
12345678910