Membrane-protein interaction and the molten globule state: interaction of alpha-lactalbumin with membranes (Q70900856)

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14 October 2019

title

Membrane-protein interaction and the molten globule state: interaction of alpha-lactalbumin with membranes (English)

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14 October 2019

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A K Lala

1

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14 October 2019

P Kaul

series ordinal

2

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14 October 2019

P B Ratnam

series ordinal

3

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14 October 2019

publication date

1 October 1995

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14 October 2019

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14 October 2019

volume

14

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14 October 2019

issue

7

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14 October 2019

page(s)

601-609

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https://scigraph.springernature.com/pub.10.1007/bf01886886

14 October 2019

exact match

0 references

cites work

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12 December 2020

The 'molten globule' state is involved in the translocation of proteins across membranes?

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12 December 2020

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12 December 2020

Alpha-lactalbumin binding to membranes: evidence for a partially buried protein.

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12 December 2020

A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A

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12 December 2020

Probing different conformational states of bovine alpha-lactalbumin: fluorescence studies with 4,4'-bis[1-(phenylamino)-8-naphthalenesulfonate].

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12 December 2020

Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin

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12 December 2020

Intercompartmental transport in the Golgi complex is a dissociative process: facile transfer of membrane protein between two Golgi populations

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12 December 2020

Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study

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12 December 2020

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Interaction of alpha-lactalbumin with phospholipid vesicles as studied by photoactivated hydrophobic labeling

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12 December 2020

Membrane proteins involved in targetted membrane fusion

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Conformation and model membrane interactions of diphtheria toxin fragment A

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12 December 2020

Metal-ion binding and the molecular conformational properties of alpha lactalbumin

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12 December 2020

Increased exposure of hydrophobic surface in molten globule state of alpha-lactalbumin. Fluorescence and hydrophobic photolabeling studies

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12 December 2020

Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies

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12 December 2020

Structural elucidation of a hydrophobic box in bovine alpha-lactalbumin by NMR: nuclear Overhauser effects.

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12 December 2020

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

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12 December 2020

Interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles. I. A microcalorimetric and fluorescence study.

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12 December 2020

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

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Influence of the protein conformation on the interaction between alpha-lactalbumin and dimyristoylphosphatidylcholine vesicles.

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12 December 2020

Identifiers

DOI

10.1007/BF01886886

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8561856%20AND%20SRC:MED&resulttype=core&format=json

14 October 2019

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