A thermodynamic analysis of a family of small globular proteins: SH3 domains (Q30167348)

9 June 2017

title

A thermodynamic analysis of a family of small globular proteins: SH3 domains (English)

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9 June 2017

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Filimonov VV

1

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9 June 2017

Azuaga AI

2

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9 June 2017

Viguera AR

3

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9 June 2017

Serrano L

4

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9 June 2017

Mateo PL

5

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9 June 2017

language of work or name

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1 March 1999

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9 June 2017

published in

Biophysical Chemistry

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9 June 2017

volume

77

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9 June 2017

issue

2-3

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9 June 2017

page(s)

195-208

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A novel viral oncogene with structural similarity to phospholipase C

9 June 2017

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Structure of the PI3K SH3 domain and analysis of the SH3 family

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Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2

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Identification of a ten-amino acid proline-rich SH3 binding site

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Characterization of the interaction of natural proline-rich peptides with five different SH3 domains.

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Molecular modeling of the interaction of polyproline-based peptides with the Abl-SH3 domain: rational modification of the interaction

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Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition.

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Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions

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Different folding transition states may result in the same native structure

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A Calorimetric Study of the Thermal Stability of Barstar and Its Interaction with Barnase

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Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin

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The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics

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Identifiers

DOI

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9 June 2017

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