(Q27735006)

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Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism (English)

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protein folding

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author name string

J L Neira

1

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B Davis

2

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A G Ladurner

3

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A M Buckle

4

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G de P Gay

5

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A R Fersht

6

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publication date

1996

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Folding & design

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1

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189-208

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3

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Protein Denaturation

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Peptide conformation and protein folding

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Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals

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Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2.

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Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds

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Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue

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Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

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Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding

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Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis

1 reference

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Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.

1 reference

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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

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Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications

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Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue

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Generation of a family of protein fragments for structure-folding studies. 2. Kinetics of association of the two chymotrypsin inhibitor-2 fragments

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Characterizing transition states in protein folding: an essential step in the puzzle

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Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2)

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The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding

1 reference

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Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.

1 reference

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Conserved residues and the mechanism of protein folding

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Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state

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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

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Amide proton titration shifts in bull seminal inhibitor IIA by two-dimensional correlated 1H nuclear magnetic resonance (COSY). Manifestation of conformational equilibria involving carboxylate groups

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'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.

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Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea.

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Protein interactions with urea and guanidinium chloride. A calorimetric study

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A structural basis for the interaction of urea with lysozyme

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Hydrophobic clustering in nonnative states of a protein: interpretation of chemical shifts in NMR spectra of denatured states of lysozyme

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Prediction of protein backbone conformation based on seven structure assignments. Influence of local interactions

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Backbone dynamics of chymotrypsin inhibitor 2: effect of breaking the active site bond and its implications for the mechanism of inhibition of serine proteases

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Conformational Pathway of the Polypeptide Chain of Chymotrypsin Inhibitor-2 Growing from its N Terminusin vitro. Parallels with the Protein Folding Pathway

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10.1016/S1359-0278(96)00031-4

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