Use of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding.
about
Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsUsing surface tension data to predict differences in surface and bulk concentrations of nonelectrolytes in water.Why Hofmeister effects of many salts favor protein folding but not DNA helix formation.The osmolyte TMAO stabilizes native RNA tertiary structures in the absence of Mg2+: evidence for a large barrier to folding from phosphate dehydration.Preferential hydration of DNA: the magnitude and distance dependence of alcohol and polyol interactionsQuantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizerAnatomy of energetic changes accompanying urea-induced protein denaturation.Its preferential interactions with biopolymers account for diverse observed effects of trehaloseDenaturation of RNA secondary and tertiary structure by urea: simple unfolded state models and free energy parameters account for measured m-values.Preferential interactions between small solutes and the protein backbone: a computational analysisQuantifying functional group interactions that determine urea effects on nucleic acid helix formation.Probing the protein-folding mechanism using denaturant and temperature effects on rate constantsDistinctive solvation patterns make renal osmolytes diverse.Interactions of the osmolyte glycine betaine with molecular surfaces in water: thermodynamics, structural interpretation, and prediction of m-values.Folding of RNA tertiary structure: Linkages between backbone phosphates, ions, and water.Late steps in the formation of E. coli RNA polymerase-lambda P R promoter open complexes: characterization of conformational changes by rapid [perturbant] upshift experiments.TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Effects of a protecting osmolyte on the ion atmosphere surrounding DNA duplexes.Effects of osmolytes on RNA secondary and tertiary structure stabilities and RNA-Mg2+ interactions.Introductory lecture: interpreting and predicting Hofmeister salt ion and solute effects on biopolymer and model processes using the solute partitioning modelKey roles of the downstream mobile jaw of Escherichia coli RNA polymerase in transcription initiation.Formation of a wrapped DNA-protein interface: experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA.Thermodynamic origin of hofmeister ion effectsSolute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subseMacromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state.Quantifying additive interactions of the osmolyte proline with individual functional groups of proteins: comparisons with urea and glycine betaine, interpretation of m-values.The mechanism and high-free-energy transition state of lac repressor-lac operator interaction.Investigation of the electrostatic and hydration properties of DNA minor groove-binding by a heterocyclic diamidine by osmotic pressure.
P2860
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P2860
Use of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Use of urea and glycine betain ...... epressor-lac operator binding.
@en
type
label
Use of urea and glycine betain ...... epressor-lac operator binding.
@en
prefLabel
Use of urea and glycine betain ...... epressor-lac operator binding.
@en
P2093
P2860
P356
P1433
P1476
Use of urea and glycine betain ...... epressor-lac operator binding.
@en
P2093
Jiang Hong
M Thomas Record
Mike W Capp
Ruth M Saecker
P2860
P304
16896-16911
P356
10.1021/BI0515218
P407
P577
2005-12-01T00:00:00Z