Crystallographic analysis of Phe→Leu substitution in the hydrophobic core of barnase
Acta Crystallogr D Biol Crystallogr
(1995)
51
220
(doi: 10.1107/S0907444994008851)
Characterizing transition states in protein folding: an essential step in the puzzle.
Current opinion in structural biology
(1995)
5
79
(doi: 10.1016/0959-440x(95)80012-p)
ASSOCIATION OF PROTEIN-FRAGMENTS THROUGH A 2ND-ORDER FOLDING REACTION - STRUCTURE OF THE ISOLATED FRAGMENTS AND EARLY EVENTS OF PROTEIN-FOLDING
PROTEIN ENGINEERING
(1995)
8
19
THE STRUCTURE OF THE TRANSITION-STATE FOR THE ASSOCIATION OF 2 FRAGMENTS OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 TO GENERATE NATIVE-LIKE PROTEIN - IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING
Proceedings of the National Academy of Sciences of the United States of America
(1994)
91
10943
(doi: 10.1073/pnas.91.23.10943)
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding
Proceedings of the National Academy of Sciences of the United States of America
(1994)
91
10422
(doi: 10.1073/pnas.91.22.10422)
Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
Proceedings of the National Academy of Sciences of the United States of America
(1994)
91
10426
(doi: 10.1073/pnas.91.22.10426)
Stability and function: two constraints in the evolution of barstar and other proteins.
Structure (London, England : 1993)
(1994)
2
945
TOWARD SOLVING THE FOLDING PATHWAY OF BARNASE - THE COMPLETE BACKBONE C-13, N-15, AND H-1-NMR ASSIGNMENTS OF ITS PH-DENATURED STATE
Proc Natl Acad Sci U S A
(1994)
91
9412
(doi: 10.1073/pnas.91.20.9412)
Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
Protein Eng
(1994)
7
1089
(doi: 10.1093/protein/7.9.1089)
Mutational analysis of the N-capping box of the alpha-helix of chymotrypsin inhibitor 2.
Protein Eng
(1994)
7
777
(doi: 10.1093/protein/7.6.777)
Pathway and Stability of Protein Folding
Biochemical Society Transactions
(1994)
22
267
(doi: 10.1042/bst0220267)
Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue.
Proceedings of the National Academy of Sciences
(1994)
91
311
(doi: 10.1073/pnas.91.1.311)
CONTRIBUTION OF A PROLINE RESIDUE AND A SALT BRIDGE TO THE STABILITY OF A TYPE-I REVERSE TURN IN CHYMOTRYPSIN INHIBITOR-2
Protein Engineering Design and Selection
(1994)
7
103
(doi: 10.1093/protein/7.1.103)
Editorial overview
Current Opinion in Structural Biology
(1994)
4
67
Contribution of Buried Hydrogen Bonds to Protein Stability The Crystal Structures of Two Barnase Mutants
Journal of molecular biology
(1993)
234
1158
(doi: 10.1006/jmbi.1993.1667)
Crystal structural analysis of mutations in the hydrophobic cores of barnase.
Journal of molecular biology
(1993)
234
847
(doi: 10.1006/jmbi.1993.1630)
Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.
Proceedings of the National Academy of Sciences
(1993)
90
9837
(doi: 10.1073/pnas.90.21.9837)
Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.
The EMBO journal
(1993)
12
4145
THE REFOLDING OF CIS-PEPTIDYLPROLYL AND TRANS-PEPTIDYLPROLYL ISOMERS OF BARSTAR
BIOCHEMISTRY-US
(1993)
32
11195
(doi: 10.1021/bi00092a032)
Protein stability: experimental data from protein engineering
Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences
(1993)
345
141
(doi: 10.1098/rsta.1993.0125)
