DOI: 10.1006/jmbi.2001.5344. Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation

Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation

10.1006/jmbi.2001.5344

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Larson, S. M., Ruczinski, I., Davidson, A. R., Baker, D., & Plaxco, K. W. (2002). Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation. Journal of Molecular Biology, 316(2), 225â233.

Authors 5

Stefan M. Larson (first)
Ingo Ruczinski (additional)
Alan R. Davidson (additional)
David Baker (additional)
Kevin W. Plaxco (additional)

References 34 Referenced 54

10.1073/pnas.92.20.9206 / Proc. Natl Acad. Sci. USA / Lattice model for rapidly folding protein-like heteropolymers by Shrivastava (1995)
10.1002/prot.340210302 / Proteins: Struct. Funct. Genet. / Funnels, pathways, and the energy landscape of protein folding by Bryngelson (1995)
10.1038/379096a0 / Nature / Conserved residues and the mechanism of protein folding by Shaknovich (1996)
10.1073/pnas.95.9.4976 / Proc. Natl Acad. Sci. USA / How evolution makes proteins fold quickly by Mirny (1998)
10.1002/pro.5560071205 / Protein Sci. / Identification of kinetically hot residues in proteins by Demirel (1998)
10.1016/S0014-5793(99)00622-5 / FEBS Letters / Predicting the protein folding nucleus from a sequence by Poupon (1999)
10.1006/jmbi.1999.2911 / J. Mol. Biol. / Universally conserved positions in protein folds by Mirny (1999)
10.1006/jmbi.2001.4602 / J. Mol. Biol. / Evolutionary conservation of the folding nucleus by Mirny (2001)
10.1146/annurev.biophys.30.1.361 / Annu. Rev. Biophys. Biomol. / Protein folding theory by Mirny (2001)
10.1006/jmbi.1999.3663 / J. Mol. Biol. / Evolutionary conservation and protein folding kinetics by Plaxco (2000)
10.1016/S0959-440X(97)80002-4 / Curr. Opin. Struct. Biol. / Nucleation mechanisms in protein folding by Fersht (1997)
10.1002/prot.340110408 / Proteins: Struct. Funct. Genet. / Information-theoretical entropy as a measure of sequence variability by Shenkin (1991)
10.1038/nsb1097-805 / Nature Struct. Biol. / Functional rapidly folding proteins from simplified amino acid sequences by Riddle (1997)
10.1073/pnas.95.9.4982 / Proc. Natl Acad. Sci. USA / The sequences of small proteins are not extensively optimized for rapid folding by natural selection by Kim (1998)
10.1016/0022-2836(80)90373-3 / J. Mol. Biol. / How different amino acid sequences determine similar protein structures by Lesk (1980)
10.1038/14901 / Nature Struct. Biol. / Experiment and theory highlight role of native state topology in SH3 folding by Riddle (1999)
10.1021/bi9817820 / Biochemistry / Effects of core mutations on the folding of a beta-sheet protein by Lorch (1999)
10.1073/pnas.96.26.14854 / Proc. Natl Acad. Sci. USA / From snapshot to movie by Ternstrom (1999)
10.1038/14890 / Nature Struct. Biol. / Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding by Chiti (1999)
10.1006/jmbi.2000.4190 / J. Mol. Biol. / Differential stabilization of the transition state of the villin 14T folding reaction by Choe (2000)
10.1016/S0969-2126(01)00596-2 / Structure / Mapping the folding pathway of an immunoglobulin domain by Fowler (2001)
10.1006/jmbi.2000.4378 / J. Mol. Biol. / The folding nucleus of a fibronectin type III domain is composed of core residues of the conserved immunoglobulin-like fold by Cota (2001)
10.1006/jmbi.2000.3517 / J. Mol. Biol. / The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology by Hamill (2000)
10.1006/jmbi.2001.4873 / J. Mol. Biol. / The folding mechanism of a β-sheet by Jäger (2001)
10.1093/nar/28.1.263 / Nucl. Acids Res. / The Pfam protein families database by Bateman (2000)
10.1093/bioinformatics/14.5.423 / Bioinformatics / Removing near-neighbor redundancy from large protein sequence collections by Holm (1998)
10.1016/0022-2836(94)90032-9 / J. Mol. Biol. / Position-based sequence weights by Henikoff (1994)
10.1110/ps.9.11.2170 / Protein Sci. / The identification of conserved interactions within the SH3 domain by alignment of sequences and structures by Larson (2000)
10.1021/bi981788p / Biochemistry / Mutagenesis of a buried polar interaction in an SH3 domain by Maxwell (1998)
10.1006/jmbi.1995.0616 / J. Mol. Biol. / The structure of the transition-state for folding of chymotrypsin inhibitor-2 analyzed by protein engineering by Itzhaki (1995)
10.1016/S1359-0278(96)00011-9 / Fold. Des. / Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2 by López-Hernández (1996)
10.1006/jmbi.1998.2158 / J. Mol. Biol. / Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain by Villegas (1998)
10.1038/9384 / Nature Struct. Biol. / The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP by Kragelund (1999)
10.1006/jmbi.1999.2942 / J. Mol. Biol. / Mapping the interactions present in the transition state for unfolding/folding of FKBP12 by Fulton (1999)

Dates

Type	When
Created	22 years, 10 months ago (Oct. 6, 2002, 2:37 p.m.)
Deposited	6 years, 3 months ago (May 8, 2019, 2:27 a.m.)
Indexed	1 year ago (Aug. 3, 2024, 2:16 p.m.)
Issued	23 years, 7 months ago (Feb. 1, 2002)
Published	23 years, 7 months ago (Feb. 1, 2002)
Published Print	23 years, 7 months ago (Feb. 1, 2002)

Funders 0

None

BibTeX

@article{Larson_2002, title={Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation}, volume={316}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.2001.5344}, DOI={10.1006/jmbi.2001.5344}, number={2}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Larson, Stefan M. and Ruczinski, Ingo and Davidson, Alan R. and Baker, David and Plaxco, Kevin W.}, year={2002}, month=feb, pages={225–233} }

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  "URL": "http://dx.doi.org/10.1006/jmbi.2001.5344",
  "relation": {
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      {
        "id-type": "doi",
        "id": "10.3410/f.1005006.58711",
        "asserted-by": "object"
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  "ISSN": [
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  "subject": [],
  "container-title-short": "Journal of Molecular Biology",
  "published": {
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}