المؤلفون: Tastan, Oznur, Dutta, Arpana, Booth, Paula, Klein-Seetharaman, Judith

المصدر: Tastan , O , Dutta , A , Booth , P & Klein-Seetharaman , J 2014 , ' Retinal proteins as model systems for membrane protein folding ' , Biochimica et Biophysica Acta , vol. 1837 , no. 5 , pp. 656-663 . https://doi.org/10.1016/j.bbabio.2013.11.021Test

مصطلحات موضوعية: Bacteriorhodopsins, Euryarchaeota, Humans, Hydrophobic and Hydrophilic Interactions, Kinetics, Molecular Dynamics Simulation, Protein Denaturation, Protein Folding, Protein Refolding, Protein Structure, Secondary, Retinaldehyde, Rhodopsin, Structural Homology, Protein, Thermodynamics

الإتاحة: https://doi.org/10.1016/j.bbabio.2013.11.021Test
https://kclpure.kcl.ac.uk/portal/en/publications/62453fa9-60de-4cdc-9641-5fdd30ab4ebbTest

المؤلفون: Tastan, Oznur, Dutta, Arpana, Booth, Paula, Klein-Seetharaman, Judith

المصدر: Tastan , O , Dutta , A , Booth , P & Klein-Seetharaman , J 2014 , ' Retinal proteins as model systems for membrane protein folding ' , Biochimica et Biophysica Acta , vol. 1837 , no. 5 , pp. 656-663 . https://doi.org/10.1016/j.bbabio.2013.11.021Test

مصطلحات موضوعية: Bacteriorhodopsins, Euryarchaeota, Humans, Hydrophobic and Hydrophilic Interactions, Kinetics, Molecular Dynamics Simulation, Protein Denaturation, Protein Folding, Protein Refolding, Protein Structure, Secondary, Retinaldehyde, Rhodopsin, Structural Homology, Protein, Thermodynamics

الإتاحة: https://doi.org/10.1016/j.bbabio.2013.11.021Test
https://kclpure.kcl.ac.uk/portal/en/publications/retinal-proteins-as-model-systems-for-membrane-protein-foldingTest(62453fa9-60de-4cdc-9641-5fdd30ab4ebb).html

المؤلفون: Booth, Paula J

المصدر: Booth , P J 2012 , ' A successful change of circumstance : a transition state for membrane protein folding ' , Current Opinion in Structural Biology , vol. 22 , no. 4 , pp. 469-475 . https://doi.org/10.1016/j.sbi.2012.03.008Test

مصطلحات موضوعية: Bacteriorhodopsins, Membrane Proteins, Models, Molecular, Protein Folding, Protein Structure, Secondary, Tertiary

الإتاحة: https://doi.org/10.1016/j.sbi.2012.03.008Test
https://kclpure.kcl.ac.uk/portal/en/publications/fce97ac0-a8f1-4266-a35f-e63e649db3c8Test

المؤلفون: Booth, Paula J

المصدر: Booth , P J 2012 , ' A successful change of circumstance : a transition state for membrane protein folding ' , Current Opinion in Structural Biology , vol. 22 , no. 4 , pp. 469-475 . https://doi.org/10.1016/j.sbi.2012.03.008Test

مصطلحات موضوعية: Bacteriorhodopsins, Membrane Proteins, Models, Molecular, Protein Folding, Protein Structure, Secondary, Tertiary

الإتاحة: https://doi.org/10.1016/j.sbi.2012.03.008Test
https://kclpure.kcl.ac.uk/portal/en/publications/a-successful-change-of-circumstanceTest(fce97ac0-a8f1-4266-a35f-e63e649db3c8).html

المؤلفون: Curnow, Paul, Di Bartolo, Natalie D, Moreton, Kathleen M, Ajoje, Oluseye O, Saggese, Nicholas P, Booth, Paula J

المصدر: Curnow , P , Di Bartolo , N D , Moreton , K M , Ajoje , O O , Saggese , N P & Booth , P J 2011 , ' Stable folding core in the folding transition state of an alpha-helical integral membrane protein ' , Proceedings of the National Academy of Sciences of the United States of America , vol. 108 , no. 34 , pp. 14133-14138 . https://doi.org/10.1073/pnas.1012594108Test

مصطلحات موضوعية: Alanine, Bacteriorhodopsins, Halobacterium salinarum, Hydrogen Bonding, Kinetics, Models, Molecular, Mutagenesis, Mutation, Protein Folding, Protein Stability, Protein Structure, Secondary, Protein Unfolding

الإتاحة: https://doi.org/10.1073/pnas.1012594108Test
https://kclpure.kcl.ac.uk/portal/en/publications/f80d2acc-a17f-460c-a8fb-8ca83438333bTest

المؤلفون: Curnow, Paul, Di Bartolo, Natalie D, Moreton, Kathleen M, Ajoje, Oluseye O, Saggese, Nicholas P, Booth, Paula J

المصدر: Curnow , P , Di Bartolo , N D , Moreton , K M , Ajoje , O O , Saggese , N P & Booth , P J 2011 , ' Stable folding core in the folding transition state of an alpha-helical integral membrane protein ' , Proceedings of the National Academy of Sciences of the United States of America , vol. 108 , no. 34 , pp. 14133-14138 . https://doi.org/10.1073/pnas.1012594108Test

مصطلحات موضوعية: Alanine, Bacteriorhodopsins, Halobacterium salinarum, Hydrogen Bonding, Kinetics, Models, Molecular, Mutagenesis, Mutation, Protein Folding, Protein Stability, Protein Structure, Secondary, Protein Unfolding

الإتاحة: https://doi.org/10.1073/pnas.1012594108Test
https://kclpure.kcl.ac.uk/portal/en/publications/stable-folding-core-in-the-folding-transition-state-of-an-alphahelical-integral-membrane-proteinTest(f80d2acc-a17f-460c-a8fb-8ca83438333b).html

المؤلفون: Curnow, Paul, Booth, Paula J

المصدر: Curnow , P & Booth , P J 2010 , ' The contribution of a covalently bound cofactor to the folding and thermodynamic stability of an integral membrane protein ' , Journal of Molecular Biology , vol. 403 , no. 4 , pp. 630-642 . https://doi.org/10.1016/j.jmb.2010.09.003Test

مصطلحات موضوعية: Bacteriorhodopsins, Detergents, Fluorescence Resonance Energy Transfer, Halobacterium salinarum, Kinetics, Lipids, Membrane Proteins, Micelles, Mutagenesis, Site-Directed, Oxadiazoles, Protein Denaturation, Protein Folding, Protein Stability, Recombinant Proteins, Retinaldehyde, Thermodynamics

الإتاحة: https://doi.org/10.1016/j.jmb.2010.09.003Test
https://kclpure.kcl.ac.uk/portal/en/publications/the-contribution-of-a-covalently-bound-cofactor-to-the-folding-and-thermodynamic-stability-of-an-integral-membrane-proteinTest(9cb8d9c5-e0dd-4037-b67e-3a53d48bd0f5).html

المؤلفون: Curnow, Paul, Booth, Paula J

المصدر: Curnow , P & Booth , P J 2010 , ' The contribution of a covalently bound cofactor to the folding and thermodynamic stability of an integral membrane protein ' , Journal of Molecular Biology , vol. 403 , no. 4 , pp. 630-642 . https://doi.org/10.1016/j.jmb.2010.09.003Test

مصطلحات موضوعية: Bacteriorhodopsins, Detergents, Fluorescence Resonance Energy Transfer, Halobacterium salinarum, Kinetics, Lipids, Membrane Proteins, Micelles, Mutagenesis, Site-Directed, Oxadiazoles, Protein Denaturation, Protein Folding, Protein Stability, Recombinant Proteins, Retinaldehyde, Thermodynamics

الإتاحة: https://doi.org/10.1016/j.jmb.2010.09.003Test
https://kclpure.kcl.ac.uk/portal/en/publications/9cb8d9c5-e0dd-4037-b67e-3a53d48bd0f5Test

المؤلفون: Dong, Mingdong, Husale, Sudhir, Sahin, Ozgur

المصدر: Dong , M , Husale , S & Sahin , O 2009 , ' Determination of protein structural flexibility by microsecond force spectroscopy ' , Nature Nanotechnology , vol. 4 , no. 8 , pp. 514-7 . https://doi.org/10.1038/nnano.2009.156Test

مصطلحات موضوعية: Bacteriorhodopsins, Cell Membrane, Halobacterium salinarum, Microscopy, Atomic Force, Electron, Scanning, Models, Chemical, Molecular, Pliability, Proteins

الإتاحة: https://doi.org/10.1038/nnano.2009.156Test
https://pure.au.dk/portal/da/publications/determination-of-protein-structural-flexibility-by-microsecond-force-spectroscopyTest(49043f50-7266-11df-8c1a-000ea68e967b).html

المؤلفون: Curnow, Paul, Booth, Paula J

المصدر: Curnow , P & Booth , P J 2007 , ' Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding ' , Proceedings of the National Academy of Sciences of the United States of America , vol. 104 , no. 48 , pp. 18970-18975 . https://doi.org/10.1073/pnas.0705067104Test

مصطلحات موضوعية: Bacteriorhodopsins, Cholic Acids, Circular Dichroism, Detergents, Dimyristoylphosphatidylcholine, Kinetics, Micelles, Protein Denaturation, Protein Structure, Secondary, Sodium Dodecyl Sulfate, Thermodynamics

الإتاحة: https://doi.org/10.1073/pnas.0705067104Test
https://kclpure.kcl.ac.uk/portal/en/publications/3100187f-6109-4ae9-8ebb-d05942fea35bTest