Calorimetric investigation of the domain structure of human complement C1.lovin.s: reversible unfolding of the short consensus repeat units

Biochemistry ◽  
1989 ◽  
Vol 28 (13) ◽  
pp. 5408-5414 ◽  
Author(s):  
Leonid V. Medved ◽  
Thomas F. Busby ◽  
Kenneth C. Ingham
Keyword(s):  
Domain Structure ◽  
Human Complement ◽  
Calorimetric Investigation ◽  
Repeat Units ◽  
Short Consensus Repeat

scholarly journals A novel short consensus repeat-containing molecule is related to human complement factor H.

1993 ◽  
Vol 268 (4) ◽  
pp. 2904-2908
Author(s):  
C. Skerka ◽  
S. Kühn ◽  
K. Günther ◽  
K. Lingelbach ◽  
P.F. Zipfel
Keyword(s):  
Factor H ◽  
Complement Factor H ◽  
Complement Factor ◽  
Human Complement ◽  
Short Consensus Repeat

scholarly journals αandβConformational preferences in fibril forming peptides characterised using NMR and CD techniques

2004 ◽  
Vol 18 (1) ◽  
pp. 1-11
Author(s):  
Thelma A. Pertinhez ◽  
Amanda K. Sherwood ◽  
Leonardo F. Fraceto ◽  
Mario Bouchard ◽  
Maureen Pitkeathly ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Strong Dependence ◽  
Short Length ◽  
Complement Receptor ◽  
Monomeric Form ◽  
Human Complement ◽  
Peptide Fragments ◽  
Native Protein ◽  
Nmr Studies ◽  
Short Consensus Repeat

Peptide fragments taken from residues 18‒54 of short consensus repeat 3 (SCR3) from the human complement receptor CR1 have been found in aqueous solution to slowly aggregate and form fibrils. NMR studies of the monomeric form of these peptides show that they are essentially unfolded in aqueous solution and that they all have an increased helicity in TFE solutions. The behaviour of residues 28‒31 from SCR3 is particularly interesting. These residues have a highβ-sheet propensity in the native protein and a seven peptide containing their sequence is found to form fibrils despite its short length. However, NMR studies show that these residues adopt a well-definedα-helix in 80% TFE and under these conditions fibril formation has not been observed. These data demonstrate the strong dependence of conformational propensities on environment.

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