The nature of the initial step in the conformational folding of disulphide-intact ribonuclease A (Q72033315)

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23 October 2019

title

The nature of the initial step in the conformational folding of disulphide-intact ribonuclease A (English)

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23 October 2019

W. A. Houry

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29 July 2024

D. M. Rothwarf

series ordinal

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29 July 2024

H. A. Scheraga

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29 July 2024

language of work or name

English

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National Center for Biotechnology Information

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29 July 2024

publication date

1 June 1995

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full work available at URL

23 October 2019

http://www.nature.com/articles/nsb0695-495.pdf

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Portable Document Format

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http://www.nature.com/articles/nsb0695-495

29 July 2024

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Nature structural biology

29 July 2024

published in

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23 October 2019

volume

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23 October 2019

issue

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23 October 2019

page(s)

495-503

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Intermediates in the folding reactions of small proteins

23 October 2019

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The barriers in protein folding

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How does protein folding get started?

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Cooperativity in protein-folding kinetics

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The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

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Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding

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Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry

31 March 2020

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Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt

31 March 2020

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Evidence for a molten globule state as a general intermediate in protein folding

31 March 2020

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Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin

31 March 2020

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A hydrophobic cluster forms early in the folding of dihydrofolate reductase

31 March 2020

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

31 March 2020

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Structure of phosphate-free ribonuclease A refined at 1.26 .ANG

31 March 2020

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Fast-folding and slow-folding forms of unfolded proteins

31 March 2020

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A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathways

31 March 2020

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pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1.

31 March 2020

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

31 March 2020

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The thermodynamic stability of proteins

31 March 2020

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Solvent denaturation and stabilization of globular proteins

31 March 2020

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Proteins as random coils. II. Hydrogen ion titration curve of ribonuclease in 6 M guanidine hydrochloride

31 March 2020

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Some factors in the interpretation of protein denaturation

31 March 2020

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31 March 2020

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inferred from DOI database lookup

7 January 2021

based on heuristic

Electrophoretic analysis of the unfolding of proteins by urea

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Protein interactions with urea and guanidinium chloride. A calorimetric study

31 March 2020

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Structural energetics of the molten globule state

31 March 2020

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Molecular basis of cooperativity in protein folding. V. Thermodynamic and structural conditions for the stabilization of compact denatured states

31 March 2020

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Toward a better understanding of protein folding pathways

31 March 2020

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Mapping the transition state and pathway of protein folding by protein engineering

31 March 2020

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31 March 2020

Folding pathway enigma

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Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

31 March 2020

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Influence of an extrinsic cross-link on the folding pathway of ribonuclease A. Kinetics of folding-unfolding

31 March 2020

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Prediction of pH-dependent properties of proteins

31 March 2020

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Hydrogen Ion Buffers for Biological Research*

31 March 2020

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31 March 2020

[3] Hydrogen ion buffers

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31 March 2020

Identifiers

DOI

10.1038/NSB0695-495

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7664113%20AND%20SRC:MED&resulttype=core&format=json

23 October 2019

1 reference

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