H
Harold D. Kim
Researcher at Stanford University
Publications - 11
Citations - 1925
Harold D. Kim is an academic researcher from Stanford University. The author has contributed to research in topics: Transfer RNA & Förster resonance energy transfer. The author has an hindex of 8, co-authored 8 publications receiving 1853 citations.
Papers
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Journal ArticleDOI
Correlating Structural Dynamics and Function in Single Ribozyme Molecules
Xiaowei Zhuang,Harold D. Kim,Miguel J. B. Pereira,Hazen P. Babcock,Nils G. Walter,Steven Chu +5 more
TL;DR: The complex structural dynamics quantitatively explain the heterogeneous cleavage kinetics common to many catalytic RNAs and the intimate coupling of structural dynamics and function is likely a general phenomenon for RNA.
Journal ArticleDOI
tRNA selection and kinetic proofreading in translation.
TL;DR: The data support a model in which ribosomal recognition of correct codon-anticodon pairs drives rotational movement of the incoming complex of EF-Tu–GTP–aa-tRNA toward peptidyl-t RNA during selection on the ribosome, and propose a mechanistic model of initial selection and proofreading.
Journal ArticleDOI
Ligand-induced conformational changes observed in single RNA molecules.
TL;DR: It is presented the first demonstration that fluorescence resonance energy transfer can be used to track the motion of a single molecule undergoing conformational changes, and it is shown that individual RNA molecules can measure the instantaneous Mg(2+) concentration with 20-ms time resolution, making it the world's smallest Mg (2+) meter.
Journal ArticleDOI
Mg2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules
TL;DR: This version of FCS/FRET on immobilized single molecules is demonstrated to be a powerful technique in the study of conformational dynamics of biomolecules over time scales ranging from microseconds to seconds.
Journal ArticleDOI
Fluorescence quenching: A tool for single-molecule protein-folding study
Xiaowei Zhuang,Taekjip Ha,Taekjip Ha,Harold D. Kim,Thomas Centner,Siegfried Labeit,Steven Chu +6 more
TL;DR: By using titin as a model system, it is demonstrated that fluorescence quenching can be used to study protein folding at the single molecule level and can signal folding and unfolding of a small protein with only one immunoglobulin domain.