Determination of the primary and secondary structures of the dromedary (Camelus dromedarius) prolactin and comparison with prolactins from other species

1991 ◽  
Vol 1077 (3) ◽  
pp. 339-345 ◽  
Author(s):  
Nadine Martinat ◽  
Jean-Claude Huet ◽  
Claude Nespoulous ◽  
Yves Combarnous ◽  
Jean-Claude Pernollet
Keyword(s):  
Secondary Structures ◽  
Camelus Dromedarius

Determination of pesticide and antibiotic residues in muscles of sudanese camel (Camelus dromedarius)

2018 ◽  
Vol 25 (2) ◽  
pp. 163 ◽  
Author(s):  
A. Ibrahim Ghada ◽  
A. Nour Ikhlas ◽  
Al-Maqbali Rabea ◽  
I.T. Kadim
Keyword(s):  
Camelus Dromedarius ◽  
Antibiotic Residues

RNA secondary structures: comparison and determination of frequently recurring substructures by consensus

1989 ◽  
Vol 5 (3) ◽  
pp. 205-210 ◽  
Author(s):  
Shu-Yun Le ◽  
John Owens ◽  
Ruth Nussinov ◽  
Jih-H. Chen ◽  
Bruce Shapiro ◽  
...  
Keyword(s):  
Secondary Structures ◽  
Rna Secondary Structures

scholarly journals Investigation of protein–protein interactions by isotope‒edited Fourier transformed infrared spectroscopy

2004 ◽  
Vol 18 (3) ◽  
pp. 397-406 ◽  
Author(s):  
Tiansheng Li
Keyword(s):  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Isotope Labeling ◽  
Structural Information ◽  
Protein Complexes ◽  
Secondary Structures ◽  
Receptor Complex ◽  
Protein Protein Interactions

Recent advance in FTIR spectroscopy has shown the usefulness of13C uniform isotope labeling in proteins to study protein–protein interactions.13C uniform isotope labeling can significantly resolve the spectral overlap in the amide I/I′ region in the spectra of protein–protein complexes, and therefore allows more accurate determination of secondary structures of individual protein component in the complex than does the conventional FTIR spectroscopy. Only a limited number of biophysical techniques can be used effectively to obtain structural information of large protein–protein complex in solution. Though X‒ray crystallography and NMR have been used to provide structural information of proteins at atomic resolution, they are limited either by the ability of protein to crystallize or the large molecular weight of protein. Vibrational spectroscopy, including FTIR and Raman spectroscopies, has been extensively employed to investigate secondary structures and conformational dynamics of protein–protein complexes. However, significant spectral overlap in the amide I/Iʹ region in the spectra of protein–protein complexes often hinders the utilization of vibrational spectroscopy in the study of protein–protein complex. In this review, we shall discuss our recent work involving the application of isotope labeled FTIR to the investigation of protein–protein complexes such as cytokine–receptor complexes. One of the examples involves G‒CSF/receptor complex. To determine unambiguously the conformations of G‒CSF and the receptor in the complex, we have prepared uniformly13C/15N isotope labeled G‒CSF to resolve its amide Iʹ band from that of its receptor in the IR spectrum of the complex. Conformational changes and structural stability of individual protein subunit in G‒CSF/receptor complex have then been investigated by using FTIR spectroscopy (Li et al.,Biochemistry29 (1997), 8849–8859). Another example involves BDNF/trkB complex in which13C/15N uniformly labeled BDNF is complexed with its receptor trkB (Li et al.,Biopolymers67(1) (2002), 10–19). Interactions of13C/15N uniformly labeled brain‒derived neurotrophic factor (BDNF) with the extracellular domain of its receptor, trkB, have been investigated by employing FTIR spectroscopy. Conformational changes and structural stability and dynamics of BDNF/trkB complex have been determined unambiguously by FTIR spectroscopy, since amide I/Iʹ bands of13C/15N labeled BDNF are resolved from those of the receptor. Together, those studies have shown that isotope edited FTIR spectroscopy can be successfully applied to the determination of protein secondary structures of protein complexes containing either the same or different types of secondary structures. It was observed that13C/15N uniform labeling also affects significantly the frequency of amide IIʹ band, which may permit the determination of hydrogen–deuterium exchange in individual subunit of protein–protein complexes.

Determination of Secondary Structures of Proteins Using Vibrational Circular Dichroism

1994 ◽  
pp. 61-70 ◽  
Author(s):  
Timothy A. Keiderling ◽  
Petr Pancoska ◽  
Vladimir Baumruk ◽  
Marie Urbanova ◽  
Vijai P. Gupta ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Secondary Structures ◽  
Vibrational Circular Dichroism ◽  
Circular Dichroïsm
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