NMR elucidation of early folding hierarchy in HIV-1 protease. (Q30332630)

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1 November 2019

title

NMR elucidation of early folding hierarchy in HIV-1 protease (English)

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1

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author name string

Ragini Sinha

series ordinal

2

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1 November 2019

P M Krishna Mohan

series ordinal

3

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1 November 2019

Ramakrishna V Hosur

series ordinal

4

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1 November 2019

language of work or name

English

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publication date

18 March 2003

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Journal of Biological Chemistry

1 November 2019

published in

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volume

278

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issue

22

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page(s)

19980-19985

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From Levinthal to pathways to funnels

1 November 2019

cites work

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Is protein folding hierarchic? II. Folding intermediates and transition states

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Making a network of hydrophobic clusters

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Confirmation of the hierarchical folding of RNase H: a protein engineering study

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Real-time NMR studies on a transient folding intermediate of barstar

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NMR characterization of partially folded and unfolded conformational ensembles of proteins

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Persistence of native-like topology in a denatured protein in 8 M urea

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

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The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions.

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Structure of the acid state of Escherichia coli ribonuclease HI.

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Role of the molten globule state in protein folding.

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Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms

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Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study

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Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin

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1.9 A x-ray study shows closed flap conformation in crystals of tethered HIV-1 PR

21 January 2018

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Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations

21 January 2018

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NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride

21 January 2018

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

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Conformation of Polypeptides and Proteins

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Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states

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Sequence-dependent correction of random coil NMR chemical shifts

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Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution

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Long-range interactions within a nonnative protein

21 January 2018

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Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin

21 January 2018

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NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding

21 January 2018

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Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding

21 January 2018

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Molecular hinges in protein folding: the urea-denatured state of apomyoglobin

21 January 2018

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NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M301615200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12644464 AND SRC:MED&resulttype=core&format=json

1 November 2019

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