Identification and Thermodynamic Characterization of Molten Globule States of Periplasmic Binding Proteins†

Biochemistry ◽  
2007 ◽  
Vol 46 (36) ◽  
pp. 10339-10352 ◽  
Author(s):  
Ravindra Singh Prajapati ◽  
S. Indu ◽  
Raghavan Varadarajan
Keyword(s):  
Binding Proteins ◽  
Molten Globule ◽  
Thermodynamic Characterization ◽  
Periplasmic Binding Proteins

scholarly journals Characterization of a Periplasmic ATP-Binding Cassette Iron Import System of Brachyspira(Serpulina) hyodysenteriae

1999 ◽  
Vol 181 (22) ◽  
pp. 6948-6957 ◽  
Author(s):  
Dominique Dugourd ◽  
Christine Martin ◽  
Clément R. Rioux ◽  
Mario Jacques ◽  
Josée Harel
Keyword(s):  
Binding Proteins ◽  
Genomic Region ◽  
Open Reading Frames ◽  
Atp Binding ◽  
Binding Motifs ◽  
Brachyspira Hyodysenteriae ◽  
Serpulina Hyodysenteriae ◽  
Periplasmic Binding Proteins ◽  
Atp Binding Cassette

ABSTRACT The nucleotide sequence of the pathogenic spirocheteBrachyspira hyodysenteriae bit (for “Brachyspira iron transport”) genomic region has been determined. The bit region is likely to encode an iron ATP-binding cassette transport system with some homology to those encountered in gram-negative bacteria. Six open reading frames oriented in the same direction and physically linked have been identified. This system possesses a protein containing ATP-binding motifs (BitD), two hydrophobic cytoplasmic membrane permeases (BitE and BitF), and at least three lipoproteins (BitA, BitB, and BitC) with homology to iron periplasmic binding proteins. These periplasmic binding proteins exhibit lipoprotein features. They are labeled by [3H]palmitate when tested in recombinantEscherichia coli, and their signal peptides are typical for substrates of the type II secretory peptidase. The FURTA system and Congo red assay indicate that BitB and BitC are involved in iron binding. The Bit system is detected only in B. hyodysenteriae and is absent from B. innocens andB. pilosicoli.

Conformational and thermodynamic characterization of the premolten globule state occurring during unfolding of the molten globule state of cytochrome c

2010 ◽  
Vol 15 (8) ◽  
pp. 1319-1329 ◽  
Author(s):  
Md. Khurshid Alam Khan ◽  
Md. Hamidur Rahaman ◽  
Md. Imtaiyaz Hassan ◽  
Tej P. Singh ◽  
Ali A. Moosavi-Movahedi ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Molten Globule ◽  
Thermodynamic Characterization ◽  
Molten Globule State

Thermodynamic characterization of liquid alloys with demixing tendency: Bi–Ga

2008 ◽  
Vol 99 (1) ◽  
pp. 18-23 ◽  
Author(s):  
Beatrix Huber ◽  
Klaus W. Richter ◽  
Hans Flandorfer ◽  
Adolf Mikula ◽  
Herbert Ipser
Keyword(s):  
Liquid Alloys ◽  
Thermodynamic Characterization
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