Terrence Gilbert Oas

Journal article J Am Chem Soc · January 22, 2014 Featured Publication Coupled ligand binding and conformational change plays a central role in biological regulation. Ligands often regulate protein function by modulating conformational dynamics, yet the order in which binding and conformational change occurs are often hotly d ... Full text Link to item Cite

Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance.

Journal article Biochemistry · November 9, 2010 Featured Publication Protein folding intermediates are often imperative for overall folding processes and consequent biological functions. However, the low population and transient nature of the intermediate states often hinder their biochemical and biophysical characterizatio ... Full text Open Access Link to item Cite

Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.

Journal article Biochemistry · June 29, 2010 Featured Publication Understanding the interconversion between thermodynamically distinguishable states present in a protein folding pathway provides not only the kinetics and energetics of protein folding but also insights into the functional roles of these states in biologic ... Full text Open Access Link to item Cite

Conformational selection or induced fit: a flux description of reaction mechanism.

Journal article Proc Natl Acad Sci U S A · August 18, 2009 Featured Publication The mechanism of ligand binding coupled to conformational changes in macromolecules has recently attracted considerable interest. The 2 limiting cases are the "induced fit" mechanism (binding first) or "conformational selection" (conformational change firs ... Full text Link to item Cite

Dynamics of backbone conformational heterogeneity in Bacillus subtilis ribonuclease P protein.

Journal article Biochemistry · December 25, 2007 Featured Publication Interconversion of protein conformations is imperative to function, as evidenced by conformational changes associated with enzyme catalytic cycles, ligand binding and post-translational modifications. In this study, we used 15N NMR relaxation experiments t ... Full text Link to item Cite

Statistical estimation of statistical mechanical models: helix-coil theory and peptide helicity prediction.

Journal article J Comput Biol · December 2007 Featured Publication Analysis of biopolymer sequences and structures generally adopts one of two approaches: use of detailed biophysical theoretical models of the system with experimentally-determined parameters, or largely empirical statistical models obtained by extracting p ... Full text Link to item Cite

Backbone dynamics of the monomeric lambda repressor denatured state ensemble under nondenaturing conditions.

Journal article Biochemistry · February 6, 2007 Featured Publication Oxidizing two native methionine residues predominantly populates the denatured state of monomeric lambda repressor (MetO-lambdaLS) under nondenaturing conditions. NMR was used to characterize the secondary structure and dynamics of MetO-lambdaLS in standar ... Full text Link to item Cite

Ligation-state hydrogen exchange: coupled binding and folding equilibria in ribonuclease P protein.

Journal article J Am Chem Soc · June 21, 2006 Featured Publication Bacillus subtilis ribonuclease P protein (P protein) is predominantly unfolded (D) at physiological pH and low ionic strength; however, small molecule anionic ligands (e.g., sulfate) directly bind to and stabilize the folded state (NL2). Because the D + 2L ... Full text Link to item Cite

Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein.

Journal article Biochemistry · October 4, 2005 Featured Publication In Bacillus subtilis, P protein is the noncatalytic component of ribonuclease P (RNase P) that is critical for achieving maximal nuclease activity under physiological conditions. P protein is predominantly unfolded (D) at neutral pH and low ionic strength; ... Full text Link to item Cite

Quantitative protein stability measurement in vivo.

Journal article Nat Struct Biol · October 2001 Featured Publication The equilibrium between the native and denatured states of a protein can be key to its function and regulation. Traditionally, the folding equilibrium constant has been measured in vitro using purified protein and simple buffers. However, the biological en ... Full text Link to item Cite

A quantitative, high-throughput screen for protein stability.

Journal article Proc Natl Acad Sci U S A · July 18, 2000 Featured Publication In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described here is a technique (referred to as SUPREX, stability of unpurified proteins from rates of H/D exchange) for measuring the ... Full text Link to item Cite

Submillisecond folding of monomeric lambda repressor.

Journal article Proc Natl Acad Sci U S A · July 18, 1995 Featured Publication The folding kinetics of a truncated form of the N-terminal domain of phage lambda repressor [lambda 6-85] has been investigated by using the technique of dynamic NMR. lambda 6-85 has been shown previously to fold in a purely two-state fashion. This allows ... Full text Link to item Cite