(Q81500061)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15756815%20AND%20SRC:MED&resulttype=core&format=json

9 January 2020

title

Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study (English)

1 reference

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9 January 2020

author name string

C Bhattacharjee

1

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9 January 2020

S Saha

2

1 reference

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9 January 2020

A Biswas

3

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9 January 2020

M Kundu

4

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9 January 2020

L Ghosh

5

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9 January 2020

K P Das

6

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9 January 2020

publication date

1 January 2005

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9 January 2020

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9 January 2020

volume

24

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9 January 2020

issue

1

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9 January 2020

page(s)

27-35

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https://scigraph.springernature.com/pub.10.1007/s10930-004-0603-z

9 January 2020

exact match

0 references

cites work

The molten globule is a third thermodynamical state of protein molecules.

1 reference

12 December 2020

Secondary structure of the hydrophobic myelin protein in a lipid environment as determined by Fourier-transform infrared spectrometry

1 reference

12 December 2020

16 The interpretation of near-ultraviolet circular dichroism

1 reference

12 December 2020

Disulfide-rearranged molten globule state of alpha-lactalbumin

1 reference

12 December 2020

The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein

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12 December 2020

Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy.

1 reference

12 December 2020

Molten globule monomer to condensed dimer: role of disulfide bonds in platelet factor-4 folding and subunit association

1 reference

12 December 2020

Redox-dependent changes in .beta.-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra

1 reference

12 December 2020

Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films

1 reference

12 December 2020

Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies.

1 reference

12 December 2020

Infrared and circular dichroism spectroscopic characterization of structural differences between beta-lactoglobulin A and B

1 reference

12 December 2020

Secondary structure and temperature behaviour of acetylcholinesterase. Studies by Fourier-transform infrared spectroscopy.

1 reference

12 December 2020

Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature

1 reference

12 December 2020

Examination of the secondary structure of proteins by deconvolved FTIR spectra

1 reference

12 December 2020

Thermal unfolding of tetrameric melittin: comparison with the molten globule state of cytochrome c

1 reference

12 December 2020

Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine beta-lactoglobulin

1 reference

12 December 2020

From Levinthal to pathways to funnels

1 reference

12 December 2020

The use and misuse of FTIR spectroscopy in the determination of protein structure

1 reference

12 December 2020

Secondary structure of the pentraxin female protein in water determined by infrared spectroscopy: effects of calcium and phosphorylcholine

1 reference

12 December 2020

New insight into protein secondary structure from resolution-enhanced infrared spectra

1 reference

12 December 2020

Dynamic structure of a highly ordered beta-sheet molten globule: multiple conformations with a stable core

1 reference

12 December 2020

Characterization of a partially structured state in an all-beta-sheet protein

1 reference

12 December 2020

Protein secondary structures in water from second-derivative amide I infrared spectra

1 reference

12 December 2020

Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry

1 reference

12 December 2020

Enhanced thermodynamic stability of beta-lactoglobulin at low pH. A possible mechanism

1 reference

12 December 2020

Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution

1 reference

12 December 2020

Modifications occur at different structural levels during the heat denaturation of beta-lactoglobulin

1 reference

12 December 2020

Aggregation of chymotrypsinogen: portrait by infrared spectroscopy

1 reference

12 December 2020

Partially folded structure of monomeric bovine β-lactoglobulin

1 reference

12 December 2020

Beware of proteins in DMSO

1 reference

12 December 2020

Thermal unfolding and refolding of beta-lactoglobulin. An intrinsic andextrinsic fluorescence study.

1 reference

12 December 2020

Infrared Spectroscopic Studies of Lyophilization‐ and Temperature‐Induced Protein Aggregation

1 reference

12 December 2020

Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment

1 reference

12 December 2020

A model for the denaturation and aggregation of beta-lactoglobulin.

1 reference

12 December 2020

Thermal denaturation of beta-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05

1 reference

12 December 2020

Redox-dependent changes in beta-sheet and loop structures of Cu,Zn superoxide dismutase in solution observed by infrared spectroscopy

1 reference

12 December 2020

Fourier transform infrared spectroscopic investigation of the interaction between myelin basic protein and dimyristoylphosphatidylglycerol bilayers

1 reference

12 December 2020

Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism

1 reference

12 December 2020

Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis

1 reference

12 December 2020

10.1007/S10930-004-0603-Z

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15756815%20AND%20SRC:MED&resulttype=core&format=json

9 January 2020

1 reference