(Q30164632)

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Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy.

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5 November 2019

Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy (English)

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5 November 2019

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5 November 2019

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Dongsheng Liu

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5 November 2019

Jinfeng Wang

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1 July 2003

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5 November 2019

Journal of Molecular Biology

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5 November 2019

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5 November 2019

821-837

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5 November 2019

describes a project that uses

NMR spectroscopy

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PABMB Lecture. Protein dynamics, folding and misfolding: from basic physical chemistry to human conformational diseases

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Chemical physics of protein folding

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Two-dimensional NMR studies of staphylococcal nuclease: evidence for conformational heterogeneity from hydrogen-1, carbon-13, and nitrogen-15 spin system assignments of the aromatic amino acids in the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+

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Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions.

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Interactions between subdomains in the partially folded state of staphylococcal nuclease

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Role of C-terminal region of Staphylococcal nuclease for foldability, stability, and activity

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Comparative studies of the conformation of the N-terminal fragments of staphylococcal nuclease R in solution

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7 January 2021

The formation and stabilization of protein structure

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Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants

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NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease

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Truncated staphylococcal nuclease is compact but disordered

1 reference

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Mutations can cause large changes in the conformation of a denatured protein.

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NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease

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7 January 2021

The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order

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7 January 2021

Residual structure in a staphylococcal nuclease fragment. Is it a molten globule and is its unfolding a first-order phase transition?

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7 January 2021

Thermodynamics of the unfolding and spectroscopic properties of the V66W mutant of Staphylococcal nuclease and its 1-136 fragment.

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Mapping the structure of a non-native state of staphylococcal nuclease

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Solution studies of staphylococcal nuclease H124L. 2. 1H, 13C, and 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphate-calcium ternary c

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A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium

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Self-association reaction of denatured staphylococcal nuclease fragments characterized by heteronuclear NMR.

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7 January 2021

Effect of salts on the stability and folding of staphylococcal nuclease

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Forcing thermodynamically unfolded proteins to fold

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Volumetric and spectroscopic characterizations of the native and acid-induced denatured states of staphylococcal nuclease.

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Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study

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Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy

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A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease

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A peptide model for proline isomerism in the unfolded state of staphylococcal nuclease

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Protein folding and unfolding at atomic resolution

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10.1016/S0022-2836(03)00660-0

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5 November 2019

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