(Q57976887)

3

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author name string

Kristofer Modig

1

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Vibeke W. Jürgensen

2

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Wolfgang Fieber

4

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Henrik G. Bohr

5

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Flemming M. Poulsen

Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing

6

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language of work or name

English

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publication date

24 September 2007

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published in

FEBS Letters

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volume

581

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issue

25

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page(s)

4965-4971

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cites work

1 reference

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The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein

21 January 2018

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Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles

21 January 2018

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Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP.

21 January 2018

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Short-range, long-range and transition state interactions in the denatured state of ACBP from residual dipolar couplings

21 January 2018

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Transient intermediary states with high and low folding probabilities in the apparent two-state folding equilibrium of ACBP at low pH.

21 January 2018

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Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein

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Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies

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Sequence-dependent correction of random coil NMR chemical shifts

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Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

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Sequence-Corrected 15N "Random Coil" Chemical Shifts

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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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Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts

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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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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol

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alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR.

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

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Long-range interactions within a nonnative protein

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The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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A relational database for sequence-specific protein NMR data

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Reversible dimerization of acid-denatured ACBP controlled by helix A4.

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3 The preparation of guanidine hydrochloride

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Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein

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The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

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