| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2007PNAS..10418970C |
| P356 | DOI | 10.1073/PNAS.0705067104 |
| P932 | PMC publication ID | 2141892 |
| P698 | PubMed publication ID | 18025476 |
| P5875 | ResearchGate publication ID | 5822694 |
| P50 | author | Paula Booth | Q21264496 |
| Paul Curnow | Q43088636 | ||
| P2093 | author name string | Paula J Booth | |
| P2860 | cites work | Side-chain contributions to membrane protein structure and stability | Q27642725 |
| Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane | Q28241677 | ||
| Rhodopsin-like protein from the purple membrane of Halobacterium halobium | Q28248225 | ||
| DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data | Q29617363 | ||
| Unravelling the folding of bacteriorhodopsin | Q34030925 | ||
| Evidence that aspartate-85 has a higher pK(a) in all-trans than in 13-cisbacteriorhodopsin | Q34040746 | ||
| Resonance Raman study of the pink membrane photochemically prepared from the deionized blue membrane of H. halobium | Q34258380 | ||
| In vitro studies of membrane protein folding | Q34499191 | ||
| Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding | Q36491309 | ||
| The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates | Q37452329 | ||
| Relationship of Leffler (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates | Q37569523 | ||
| Cation binding by bacteriorhodopsin | Q37674109 | ||
| Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation | Q37684251 | ||
| Chromophore equilibria in bacteriorhodopsin | Q39724167 | ||
| All-trans to 13-cis retinal isomerization in light-adapted bacteriorhodopsin at acidic pH. | Q43964212 | ||
| Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication | Q44438025 | ||
| A method for assessing the stability of a membrane protein. | Q45956650 | ||
| Crystal structures of acid blue and alkaline purple forms of bacteriorhodopsin. | Q50483833 | ||
| Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin. | Q50779615 | ||
| Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple‐to‐blue transition of bacteriorhodopsin A solid‐state13C CP‐MAS NMR investigation | Q50793137 | ||
| Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation. | Q50804322 | ||
| The purple to blue transition of bacteriorhodopsin is accompanied by a loss of the hexagonal lattice and a conformational change. | Q50884828 | ||
| Induction of the blue form of bacteriorhodopsin by low concentrations of sodium dodecyl sulfate. | Q50924405 | ||
| Identification of retinal isomers isolated from bacteriorhodopsin | Q54538030 | ||
| How do small single-domain proteins fold? | Q55067789 | ||
| The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH 1 1Edited by A. R. Fersht | Q57905244 | ||
| Slow α Helix Formation during Folding of a Membrane Protein† | Q57905247 | ||
| Retinal Binding during Folding and Assembly of the Membrane Protein Bacteriorhodopsin† | Q57905249 | ||
| Intermediates in the folding of the membrane protein bacteriorhodopsin | Q59488899 | ||
| Chemical modification of bacteriorhodopsin with N-bromosuccinimide | Q67654185 | ||
| Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra | Q68554855 | ||
| Structure and thermal stability of monomeric bacteriorhodopsin in mixed phospholipid/detergent micelles | Q69658326 | ||
| Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures | Q70373352 | ||
| Salt and pH-dependent changes of the purple membrane absorption spectrum | Q70722300 | ||
| Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments | Q70729927 | ||
| Formation of 9-cis- and 11-cis-retinal pigments from bacteriorhodopsin by irradiating purple membrane in acid | Q71289803 | ||
| Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions | Q73187875 | ||
| Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy | Q73502636 | ||
| P433 | issue | 48 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | membrane protein | Q423042 |
| P304 | page(s) | 18970-18975 | |
| P577 | publication date | 2007-11-19 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding | |
| P478 | volume | 104 |
| Q39333393 | Applications of Single-Molecule Methods to Membrane Protein Folding Studies |
| Q39810882 | Architectural and thermodynamic principles underlying intramembrane protease function |
| Q43082430 | Bacteriorhodopsin folds through a poorly organized transition state |
| Q88233126 | Bicelle size modulates the rate of bacteriorhodopsin folding |
| Q35818607 | Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops. |
| Q30153423 | Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial β-barrel anion channel hVDAC-2 |
| Q30153331 | Differential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis |
| Q64244254 | Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis |
| Q36301143 | Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES. |
| Q37373862 | Folding scene investigation: membrane proteins |
| Q34998163 | In vitro folding and assembly of the Escherichia coli ATP-binding cassette transporter, BtuCD |
| Q30153438 | Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2 |
| Q48089406 | Interaction Between Luteinizing Hormone-Releasing Hormone and GM1-Doped Cholesterol/Sphingomyelin Vesicles: A Spectroscopic Study. |
| Q38687156 | Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles |
| Q30153289 | Juxtamembrane tryptophans have distinct roles in defining the OmpX barrel-micelle boundary and facilitating protein-micelle association |
| Q47787076 | Kinetic stability of membrane proteins |
| Q30153375 | Kinetics and thermodynamics of membrane protein folding |
| Q50063713 | Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein. |
| Q41910574 | Malleability of the folding mechanism of the outer membrane protein PagP: parallel pathways and the effect of membrane elasticity |
| Q37180083 | Mapping the energy landscape for second-stage folding of a single membrane protein |
| Q54376952 | Mapping the folding pathway of the transmembrane protein DsbB by protein engineering |
| Q37474879 | Measuring membrane protein stability under native conditions |
| Q36692899 | Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm |
| Q37340435 | Membrane proteins can have high kinetic stability |
| Q30375584 | Methods for measuring the thermodynamic stability of membrane proteins. |
| Q51038981 | Model for coupled insertion and folding of membrane-spanning proteins. |
| Q42565526 | Primary and secondary dimer interfaces of the fibroblast growth factor receptor 3 transmembrane domain: characterization via multiscale molecular dynamics simulations. |
| Q34575556 | Probing membrane protein unfolding with pulse proteolysis. |
| Q37681352 | Protein folding in membranes. |
| Q42174627 | Protein structural dynamics at the gas/water interface examined by hydrogen exchange mass spectrometry |
| Q40359573 | Refining the treatment of membrane proteins by coarse-grained models |
| Q39425995 | Reversible folding of human peripheral myelin protein 22, a tetraspan membrane protein |
| Q42550769 | Revisiting the folding kinetics of bacteriorhodopsin. |
| Q37234128 | Sequential steps in the assembly of the multimeric outer membrane secretin PulD |
| Q27656426 | Similar Energetic Contributions of Packing in the Core of Membrane and Water-Soluble Proteins |
| Q42911823 | Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry |
| Q35180786 | Stable folding core in the folding transition state of an alpha-helical integral membrane protein. |
| Q34690261 | Structural changes in bacteriorhodopsin during in vitro refolding from a partially denatured state |
| Q38274771 | Targeting acidity in diseased tissues: mechanism and applications of the membrane-inserting peptide, pHLIP. |
| Q43503107 | The Contribution of a Covalently Bound Cofactor to the Folding and Thermodynamic Stability of an Integral Membrane Protein |
| Q38270911 | The safety dance: biophysics of membrane protein folding and misfolding in a cellular context |
| Q30156968 | The transition state for folding of an outer membrane protein |
| Q37070525 | The transition state for integral membrane protein folding |
| Q30373092 | Thermal Stability of Dopamine Transporters. |
| Q40851291 | Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state. |
| Q34276447 | Unfolding free energy of a two-domain transmembrane sugar transport protein |
| Q42727017 | Unfolding study of a trimeric membrane protein AcrB. |