DOI: 10.1016/s1359-0278(97)00008-4. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude

Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude

10.1016/s1359-0278(97)00008-4

Crossref journal-article

Elsevier BV

Folding and Design (78)

Bibliography

Munson, M., Anderson, K. S., & Regan, L. (1997). Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Folding and Design, 2(1), 77â87.

Authors 3

Mary Munson (first)
Karen S. Anderson (additional)
Lynne Regan (additional)

References 29 Referenced 54

10.1051/jcp/1968650044 / J. Chim. Phys / Are there pathways for protein folding? by Levinthal (1968)
10.1073/pnas.93.7.2627 / Proc. Natl. Acad. Sci. USA / Why is protein folding so fast? by Baldwin (1996)
10.1021/bi00358a035 / Biochemistry / Effects of the phenylalanine-22 → leucine, glutamic acid-49 → methionine, glycine-234 → aspartic acid, and glycine-234 → lysine mutations on the folding and stability of the α subunit of tryptophan synthase from Escherichia coli by Beasty (1986)
10.1021/bi00145a003 / Biochemistry / Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy by Elöve (1992)
10.1146/annurev.bi.59.070190.003215 / Annu. Rev. Biochem / Intermediates in the folding reactions of small proteins by Kim (1990)
10.1021/bi00107a010 / Biochemistry / Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition by Jackson (1991)
10.1021/bi00120a025 / Biochemistry / Folding kinetics of T4 lysozyme and nine mutants at 12°C by Chen (1992)
10.1016/0022-2836(92)90563-Y / J. Mol. Biol / The folding of an enzyme III. Structure of the transition state for unfolding of barnase analyzed by a protein engineering procedure by Serrano (1992)
10.1038/nsb0895-663 / Nat. Struct. Biol / Extremely rapid protein folding in the absence of intermediates by Schindler (1995)
10.1021/bi00482a009 / Biochemistry / Folding and stability of trp aporepressor from Escherichia coli by Gittelman (1990)
10.1021/bi00171a011 / Biochemistry / P22 Arc repressor: folding kinetics of a single-domain, dimeric protein by Milla (1994)
10.1021/bi00012a028 / Biochemistry / Kinetics of folding of leucine zipper domains by Wendt (1995)
10.1021/bi00039a042 / Biochemistry / Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy by Zitzewitz (1995)
10.1073/pnas.93.7.2629 / Proc. Natl. Acad. Sci. USA / Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure by Waldburger (1996)
10.1038/nsb0896-711 / Nat. Struct. Biol / The dimeric DNA binding domain of the human papillomavirus E2 protein folds through a monomeric intermediate which cannot be native-like by Mok (1996)
10.1016/0968-0004(85)90168-9 / Trends Biochem. Sci / Regulation of plasmid copy number by complementary RNAs by Cesareni (1985)
10.1126/science.7539549 / Science / Bent helix formation between RNA hairpins with complementary loops by Marino (1995)
10.1002/pro.5560031114 / Protein Sci / Redesigning the hydrophobic core of a four-helix-bundle protein by Munson (1994)
10.1002/pro.5560050813 / Protein Sci / What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties by Munson (1996)
10.1002/bip.1973.360121107 / Biopolymers / Kinetics of thermal unfolding of lysozyme by Segawa (1973)
10.1021/bi00314a001 / Biochemistry / Protein folding kinetics from magnetization transfer nuclear magnetic resonance by Dobson (1984)
10.1021/bi00042a024 / Biochemistry / P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding by Milla (1995)
10.1021/bi00428a042 / Biochemistry / Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations by Chen (1989)
10.1016/0092-8674(95)90449-2 / Cell / Dissecting RNA–protein interactions: RNA–RNA recognition by Rop by Predki (1995)
10.1021/jo00008a014 / J. Org. Chem / Selective reduction of disulfides by tris(2-carboxyethyl) phosphine by Burns (1991)
10.1016/0022-2836(87)90039-8 / J. Mol. Biol / Structure of the ColE1 Rop protein at 1.7 Å resolution by Banner (1987)
10.1016/0378-1119(94)90203-8 / Gene / ColE1-compatible vectors for high-level expression of cloned DNAs from the T7 promoter by Munson (1994)
{'key': '10.1016/S1359-0278(97)00008-4_bib28', 'series-title': 'Physical Chemistry: Principles and Applications in Biological Sciences', 'author': 'Tinoco', 'year': '1985'} / Physical Chemistry: Principles and Applications in Biological Sciences by Tinoco (1985)
10.1107/S0021889891004399 / J. Appl. Crystallogr / Molscript: a program to produce both detailed and schematic plots of protein structures by Kraulis (1991)

Dates

Type	When
Created	20 years, 1 month ago (July 7, 2005, 11:24 a.m.)
Deposited	6 years, 5 months ago (March 5, 2019, 12:49 p.m.)
Indexed	1 year ago (Aug. 12, 2024, 4:34 a.m.)
Issued	28 years, 6 months ago (Feb. 1, 1997)
Published	28 years, 6 months ago (Feb. 1, 1997)
Published Print	28 years, 6 months ago (Feb. 1, 1997)

Funders 0

None

BibTeX

@article{Munson_1997, title={Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude}, volume={2}, ISSN={1359-0278}, url={http://dx.doi.org/10.1016/s1359-0278(97)00008-4}, DOI={10.1016/s1359-0278(97)00008-4}, number={1}, journal={Folding and Design}, publisher={Elsevier BV}, author={Munson, Mary and Anderson, Karen S. and Regan, Lynne}, year={1997}, month=feb, pages={77–87} }

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