Folding & design: Introduction to a new journal
FOLDING & DESIGN
(1996)
1
U7
Folding & Design: introduction to a new journal.
Structure
(1996)
1
i
Pathways of protein folding
PROG BIOPHYS MOL BIO
(1996)
65
SA401
Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway.
Journal of molecular biology
(1995)
254
968
(doi: 10.1006/jmbi.1995.0669)
Perturbed pKA-values in the Denatured States of Proteins
J Mol Biol
(1995)
254
980
(doi: 10.1006/jmbi.1995.0670)
Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.
Journal of molecular biology
(1995)
254
289
(doi: 10.1006/jmbi.1995.0617)
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
J Mol Biol
(1995)
254
260
(doi: 10.1006/jmbi.1995.0616)
A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding
J Mol Biol
(1995)
254
305
(doi: 10.1006/jmbi.1995.0618)
Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.
Proc Natl Acad Sci U S A
(1995)
92
10869
(doi: 10.1073/pnas.92.24.10869)
Submillisecond events in protein folding.
Proceedings of the National Academy of Sciences
(1995)
92
10668
(doi: 10.1073/pnas.92.23.10668)
Disulfide Mutants of Barnase II: Changes in Structure and Local Stability Identified by Hydrogen Exchange
Journal of molecular biology
(1995)
253
505
(doi: 10.1006/jmbi.1995.0569)
Disulfide Mutants of Barnase I: Changes in Stability and Structure Assessed by Biophysical Methods and X-ray Crystallography
Journal of molecular biology
(1995)
253
493
(doi: 10.1006/jmbi.1995.0568)
Negative activation enthalpies in the kinetics of protein folding.
Proceedings of the National Academy of Sciences
(1995)
92
8926
(doi: 10.1073/pnas.92.19.8926)
The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.
Proc Natl Acad Sci U S A
(1995)
92
5326
(doi: 10.1073/pnas.92.12.5326)
Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution.
Philos Trans R Soc Lond B Biol Sci
(1995)
348
11
(doi: 10.1098/rstb.1995.0040)
Preface
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(1995)
348
3
(doi: 10.1098/rstb.1995.0038)
Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles.
J Mol Biol
(1995)
248
478
Folding of a nascent polypeptide chain in vitro: Cooperative formation of structure in a protein module
Proc Natl Acad Sci U S A
(1995)
92
3683
(doi: 10.1073/pnas.92.9.3683)
TOWARD SOLVING THE FOLDING PATHWAY OF BARNASE - THE BACKBONE C-13, N-15 AND H-1-NMR ASSIGNMENTS OF ITS PH-DENATURED AND UREA-DENATURED STATES
J CELL BIOCHEM
(1995)
42
Crystallographic analysis of Phe→Leu substitution in the hydrophobic core of barnase
Acta Crystallographica Section D, Structural Biology
(1995)
51
220
(doi: 10.1107/S0907444994008851)
