DOI: 10.1016/s1359-0278(97)00050-3. Strain in the folding nucleus of chymotrypsin inhibitor 2

Strain in the folding nucleus of chymotrypsin inhibitor 2

10.1016/s1359-0278(97)00050-3

Crossref journal-article

Elsevier BV

Folding and Design (78)

Bibliography

Ladurner, A. G., Itzhaki, L. S., & Fersht, A. R. (1997). Strain in the folding nucleus of chymotrypsin inhibitor 2. Folding and Design, 2(6), 363â368.

Authors 3

Andreas G Ladurner (first)
Laura S Itzhaki (additional)
Alan R Fersht (additional)

References 42 Referenced 25

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10.1002/pro.5560031106 / Protein Sci / Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G by Kuszewski (1994)
10.1073/pnas.92.15.6878 / Proc. Natl Acad. Sci. USA / Submillisecond folding of monomeric lambda repressor by Huang (1995)
10.1038/nsb0895-663 / Nat. Struct. Biol / Extremely rapid folding in the absence of intermediates by Schindler (1995)
10.1021/bi00021a037 / Biochemistry / Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein by Kragelund (1995)
10.1073/pnas.92.24.10869 / Proc. Natl Acad. Sci. USA / Optimization of rates of protein folding: the nucleation-collapse mechanism for the folding of chymotrypsin inhibitor 2 (CI2) and its consequences by Fersht (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)
10.1016/S1359-0278(97)00003-5 / Fold. Des / Favourable native-like helical local interactions can accelerate protein folding by Viguera (1997)
10.1073/pnas.94.11.5622 / Proc. Natl Acad. Sci. USA / Diffusion control in an elementary protein folding reaction by Jacob (1997)
10.1038/nsb0497-305 / Nat. Struct. Biol / The energy landscape of a fast-folding protein mapped by Ala→Gly substitutions by Burton (1997)
10.1016/S1359-0278(96)00033-8 / Fold. Des / Improved design of stable and fast-folding model proteins by Abkevich (1996)
10.1038/379096a0 / Nature / Conserved residues and the mechanism of protein-folding by Shakhnovich (1996)
10.1016/S1359-0278(96)00019-3 / Fold. Des / Universality and diversity of the protein folding scenarios: a comprehensive analysis with the aid of a lattice model by Mirny (1996)
10.1016/S1359-0278(96)00060-0 / Fold. Des / Protein folding funnels: the nature of the transition state ensemble by Onuchic (1996)
10.1016/S1074-5521(96)90090-3 / Chem. Biol / Fast folding experiments and the topography of protein-folding energy landscapes by Wolynes (1996)
10.1073/pnas.91.22.10422 / Proc. Natl Acad. Sci. USA / The structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor-2 and its implications for mechanisms of protein folding by Otzen (1994)
10.1006/jmbi.1995.0616 / J. Mol. Biol / The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods — evidence for a nucleation-condensation mechanism for protein-folding by Itzhaki (1995)
10.1006/jmbi.1995.0617 / J. Mol. Biol / Search for nucleation sites in small fragments of chymotrypsin inhibitor-2 by Itzhaki (1995)
10.1006/jmbi.1995.0669 / J. Mol. Biol / Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N-terminus in vitro by de Prat Gay (1995)
10.1006/jmbi.1997.0932 / J. Mol. Biol / Following cooperative formation of secondary and tertiary structure in a single protein module by Neira (1997)
10.1016/0076-6879(91)02008-W / Methods Enzymol / Protein engineering in analysis of protein folding pathways and stability by Matouschek (1991)
10.1006/jmbi.1996.0173 / J. Mol. Biol / Structure of the transition state for folding of a protein derived from experiment and simulation by Daggett (1996)
10.1006/jmbi.1996.0172 / J. Mol. Biol / Identification and characterization of the unfolding transition-state of chymotrypsin inhibitor 2 by molecular dynamics simulations by Li (1996)
10.1073/pnas.94.3.777 / Proc. Natl Acad. Sci. USA / Structural correlations in protein folding funnels by Shoemaker (1997)
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10.1002/pro.5560020811 / Protein Sci / Hydrophobic core repacking and aromatic–aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117→Phe by Anderson (1993)
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Dates

Type	When
Created	20 years, 1 month ago (July 7, 2005, 11:24 a.m.)
Deposited	6 years, 7 months ago (Jan. 24, 2019, 12:50 p.m.)
Indexed	1 year ago (Aug. 4, 2024, 7:56 a.m.)
Issued	27 years, 9 months ago (Dec. 1, 1997)
Published	27 years, 9 months ago (Dec. 1, 1997)
Published Print	27 years, 9 months ago (Dec. 1, 1997)

Funders 0

None

BibTeX

@article{Ladurner_1997, title={Strain in the folding nucleus of chymotrypsin inhibitor 2}, volume={2}, ISSN={1359-0278}, url={http://dx.doi.org/10.1016/s1359-0278(97)00050-3}, DOI={10.1016/s1359-0278(97)00050-3}, number={6}, journal={Folding and Design}, publisher={Elsevier BV}, author={Ladurner, Andreas G and Itzhaki, Laura S and Fersht, Alan R}, year={1997}, month=dec, pages={363–368} }

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