Three-dimensional structure and biological function of transfer RNA

1977 ◽  
Vol 10 (11) ◽  
pp. 388-396 ◽  
Author(s):  
Alexander Rich
Keyword(s):  
Biological Function ◽  
Three Dimensional ◽  
Transfer Rna ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Three-dimensional structure of yeast phenylalanine transfer RNA at 3. 0Å resolution

Nature ◽  
1974 ◽  
Vol 248 (5443) ◽  
pp. 20-24 ◽  
Author(s):  
F. L. Suddath ◽  
G. J. Quigley ◽  
A. McPherson ◽  
D. Sneden ◽  
J. J. Kim ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Transfer Rna ◽  
Dimensional Structure ◽  
Three Dimensional Structure

The dark and bright sides of an enzyme: a three dimensional structure of the N-terminal domain of Zophobas morio luciferase-like enzyme, inferences on the biological function and origin of oxygenase/luciferase activity

2016 ◽  
Vol 15 (5) ◽  
pp. 654-665 ◽  
Author(s):  
R. A. Prado ◽  
C. R. Santos ◽  
D. I. Kato ◽  
M. T. Murakami ◽  
V. R. Viviani
Keyword(s):  
Biological Function ◽  
Luciferase Activity ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Catalytic Residue ◽  
Three Dimensional Structure ◽  
Catalytic Activities ◽  
Terminal Domain ◽  
Coa Ligase

The structure and catalytic activities of a Malpighian luciferase-like enzyme indicate a generalistic xenobiotic CoA-ligase and a catalytic residue for bioluminescence.

scholarly journals The Three-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Shape of the Molecule at 5.5-A Resolution

1972 ◽  
Vol 69 (12) ◽  
pp. 3746-3750 ◽  
Author(s):  
S. H. Kim ◽  
G. Quigley ◽  
F. L. Suddath ◽  
A. McPherson ◽  
D. Sneden ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Transfer Rna ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Low-complexity sequences and single amino acid repeats: not just “junk” peptide sequences

Genome ◽  
2010 ◽  
Vol 53 (10) ◽  
pp. 753-762 ◽  
Author(s):  
Wilfried Haerty ◽  
G. Brian Golding
Keyword(s):  
Biological Function ◽  
Three Dimensional ◽  
Size Variation ◽  
Low Complexity ◽  
Single Amino Acid ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Amino Acid Repeats ◽  
Eukaryotic Proteomes ◽  
Definition Of

For decades proteins were thought to interact in a “lock and key” system, which led to the definition of a paradigm linking stable three-dimensional structure to biological function. As a consequence, any non-structured peptide was considered to be nonfunctional and to evolve neutrally. Surprisingly, the most commonly shared peptides between eukaryotic proteomes are low-complexity sequences that in most conditions do not present a stable three-dimensional structure. However, because these sequences evolve rapidly and because the size variation of a few of them can have deleterious effects, low-complexity sequences have been suggested to be the target of selection. Here we review evidence that supports the idea that these simple sequences should not be considered just “junk” peptides and that selection drives the evolution of many of them.

Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase

Science ◽  
1984 ◽  
Vol 226 (4680) ◽  
pp. 1315-1317 ◽  
Author(s):  
T Webster ◽  
H Tsai ◽  
M Kula ◽  
G. Mackie ◽  
P Schimmel
Keyword(s):  
Sequence Homology ◽  
Three Dimensional ◽  
Transfer Rna ◽  
Dimensional Structure ◽  
Specific Sequence ◽  
Three Dimensional Structure ◽  
Aminoacyl Transfer

Three-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Folding of the Polynucleotide Chain

Science ◽  
1973 ◽  
Vol 179 (4070) ◽  
pp. 285-288 ◽  
Author(s):  
S. H. Kim ◽  
G. J. Quigley ◽  
F. L. Suddath ◽  
A. McPherson ◽  
D. Sneden ◽  
...  
Keyword(s):  
Rna Folding ◽  
Three Dimensional ◽  
Transfer Rna ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Polynucleotide Chain
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