DOI: 10.1016/j.jmb.2003.07.002. Multiple Parallel-pathway Folding of Proline-free Staphylococcal Nuclease

Multiple Parallel-pathway Folding of Proline-free Staphylococcal Nuclease

10.1016/j.jmb.2003.07.002

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Kamagata, K., Sawano, Y., Tanokura, M., & Kuwajima, K. (2003). Multiple Parallel-pathway Folding of Proline-free Staphylococcal Nuclease. Journal of Molecular Biology, 332(5), 1143â1153.

Authors 4

Kiyoto Kamagata (first)
Yoriko Sawano (additional)
Masaru Tanokura (additional)
Kunihiro Kuwajima (additional)

References 28 Referenced 41

10.1073/pnas.92.20.9029 / Proc. Natl. Acad. Sci. USA / Kinetic traps in lysozyme folding by Kiefhaber (1995)
10.1006/jmbi.1997.1030 / J. Mol. Biol. / Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate by Wildegger (1997)
10.1021/bi00065a034 / Biochemistry / A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model by Jennings (1993)
10.1006/jmbi.2001.5230 / J. Mol. Biol. / Highly divergent dihydrofolate reductases conserve complex folding mechanisms by Wallace (2002)
10.1038/87624 / Nature Struct. Biol. / Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics by Pappenberger (2001)
10.1002/prot.340100203 / Proteins: Struct. Funct. Genet. / The crystal structure of staphylococcal nuclease refined at 1.7Å resolution by Hynes (1991)
10.1126/science.167.3919.886 / Science / Kinetics of folding of staphylococcal nuclease by Schechter (1970)
10.1021/bi00224a018 / Biochemistry / Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra by Sugawara (1991)
10.1016/0014-5793(91)81243-2 / FEBS Letters / The Pro117 to glycine mutation of staphylococcal nuclease simplifies the unfolding–folding kinetics by Kuwajima (1991)
10.1073/pnas.91.2.449 / Proc. Natl. Acad. Sci. USA / Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy by Jacobs (1994)
10.1021/bi9700476 / Biochemistry / Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease by Walkenhorst (1997)
10.1021/bi963174v / Biochemistry / Kinetic folding and cis/trans prolyl isomerization of staphylococcal nuclease. A study by stopped-flow absorption, stopped-flow circular dichroism and molecular dynamics simulations by Ikura (1997)
10.1021/bi981962+ / Biochemistry / Effects of proline mutations on the folding of staphylococcal nuclease by Maki (1999)
{'key': '10.1016/j.jmb.2003.07.002_BIB14', 'series-title': 'Old and New Views of Protein Folding', 'first-page': '271', 'article-title': 'Equilibrium and kinetics of folding of staphylococcal nuclease and its proline mutants', 'author': 'Maki', 'year': '1999'} / Old and New Views of Protein Folding / Equilibrium and kinetics of folding of staphylococcal nuclease and its proline mutants by Maki (1999)
10.1110/ps.ps.28202 / Protein Sci. / Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange by Walkenhorst (2002)
10.1021/ja980181t / J. Am. Chem. Soc. / Barriers to rotation of secondary amide peptide bonds by Scherer (1998)
10.1016/S0022-2836(95)80039-5 / J. Mol. Biol. / Non-prolyl cis–trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding by Odefey (1995)
10.1128/jb.169.2.751-757.1987 / J. Bacteriol. / Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure by Ben-Bassat (1987)
10.1093/protein/11.5.333 / Protein Eng. / Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue by Ishikawa (1998)
10.1006/jmbi.1998.2362 / J. Mol. Biol. / Effect of the extra N-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli by Chaudhuri (1999)
10.1073/pnas.96.6.2782 / Proc. Natl. Acad. Sci. USA / Multiple pathways on a protein-folding energy landscape: kinetic evidence by Goldbeck (1999)
10.1093/emboj/18.17.4794 / EMBO J. / The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase by van den Berg (1999)
10.1006/jmbi.2001.4804 / J. Mol. Biol. / Origin of apparent fast and non-exponential kinetics of lysozyme folding measured in pulsed hydrogen exchange experiments by Bieri (2001)
10.1021/bi9909703 / Biochemistry / A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding by Bieri (1999)
10.1073/pnas.91.22.10426 / Proc. Natl. Acad. Sci. USA / Single versus parallel pathways of protein folding and fractional formation of structure in the transition state by Fersht (1994)
10.1155/2003/252581 / Spectrosc. Intl J. / Parallel folding pathway of proline-free staphylococcal nuclease studied by the stopped-flow double-jump method by Kamagata (2003)
10.1016/0003-2697(80)90211-0 / Anal. Biochem. / Calibration of stopped-flow spectrophotometers using a two-step disulfide exchange reaction by Paul (1980)
10.1016/0003-2697(89)90235-2 / Anal. Biochem. / Determination of the dead time of a stopped-flow fluorometer by Brissette (1989)

Dates

Type	When
Created	21 years, 11 months ago (Sept. 16, 2003, 7:53 p.m.)
Deposited	6 years, 6 months ago (Feb. 24, 2019, 2:52 a.m.)
Indexed	1 month ago (Aug. 2, 2025, 1:09 a.m.)
Issued	21 years, 11 months ago (Oct. 1, 2003)
Published	21 years, 11 months ago (Oct. 1, 2003)
Published Print	21 years, 11 months ago (Oct. 1, 2003)

Funders 0

None

BibTeX

@article{Kamagata_2003, title={Multiple Parallel-pathway Folding of Proline-free Staphylococcal Nuclease}, volume={332}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2003.07.002}, DOI={10.1016/j.jmb.2003.07.002}, number={5}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Kamagata, Kiyoto and Sawano, Yoriko and Tanokura, Masaru and Kuwajima, Kunihiro}, year={2003}, month=oct, pages={1143–1153} }

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