Aminoacyl-tRNA synthesis
▪ Abstract Aminoacyl-tRNAs are substrates for translation and are pivotal in determining how
the genetic code is interpreted as amino acids. The function of aminoacyl-tRNA synthesis is …
the genetic code is interpreted as amino acids. The function of aminoacyl-tRNA synthesis is …
Hydrogen bonding and chemical reactivity
F Hibbert, J Emsley - Advances in physical organic chemistry, 1990 - Elsevier
Publisher Summary This chapter discusses the hydrogen bonding, which has been
recognized as the single most important intermolecular interaction, The chapter presents the …
recognized as the single most important intermolecular interaction, The chapter presents the …
[图书][B] Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding
A Fersht - 1999 - books.google.com
The three-dimensional structure of proteins. Chemical catalysis. The basic equations of
enzyme kinetics. Measurement and magnitude of individual rate constants. The pH …
enzyme kinetics. Measurement and magnitude of individual rate constants. The pH …
Hydrogen bonding and biological specificity analysed by protein engineering
AR Fersht, JP Shi, J Knill-Jones, DM Lowe… - Nature, 1985 - nature.com
The role of complementary hydrogen bonding as a determinant of biological specificity has
been examined by protein engineering of the tyrosyl-tRNA synthetase. Deletion of a side …
been examined by protein engineering of the tyrosyl-tRNA synthetase. Deletion of a side …
The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
In a previous study, a mutant of tyrosyl-tRNA synthetase in which a threonine residue
(Thr51) was converted to proline dramatically improved the aff inity of the enzyme for its ATP …
(Thr51) was converted to proline dramatically improved the aff inity of the enzyme for its ATP …
Structure of E. coli Glutaminyl-tRNA Synthetase Complexed with tRNAGln and ATP at 2.8 Å Resolution
The crystal structure of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) complexed with
its cognate glutaminyl transfer RNA (tRNAGln) and adenosine triphosphate (ATP) has been …
its cognate glutaminyl transfer RNA (tRNAGln) and adenosine triphosphate (ATP) has been …
The role of the α-helix dipole in protein function and structure
WGJ Hol - Progress in Biophysics and Molecular biology, 1985 - Elsevier
The role of the α-helix dipole in protein function and structure - ScienceDirect Skip to main
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Structural studies of protein–nucleic acid interaction: the sources of sequence-specific binding
TA Steitz - Quarterly reviews of biophysics, 1990 - cambridge.org
Structural studies of DNA-binding proteins and their complexes with DNA have proceeded at
an accelerating pace in recent years due to important technical advances in molecular …
an accelerating pace in recent years due to important technical advances in molecular …
Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding
G Winter, AR Fersht, AJ Wilkinson, M Zoller, M Smith - Nature, 1982 - nature.com
We describe here a general method for systematically replacing amino acids in an enzyme.
This allows analysis of their molecular roles in substrate binding or catalysis and could …
This allows analysis of their molecular roles in substrate binding or catalysis and could …
Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolution: Interaction of the enzyme with the tyrosyl adenylate intermediate
P Brick, TN Bhat, DM Blow - Journal of molecular biology, 1989 - Elsevier
The crystal structure of tyrosyl-tRNA synthetase (EC 6.1. 1.1) from Bacillus
stearothermophilus has been refined to a crystallographic R-factor of 22.6% at 2.3 Å …
stearothermophilus has been refined to a crystallographic R-factor of 22.6% at 2.3 Å …