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J. Biol. Chem., Vol. 265, Issue 17, 10081-10087, 06, 1990
NP Morris, SL Watt, JM Davis and HP Bachinger
The thermal triple helix to coil transitions of two human type V collagens
(alpha 1(2) alpha 2 and alpha 1 alpha 2 alpha 3) and bovine type XI
collagen differ from those of the interstitial collagens type I, II, and
III by the presence of unfolding intermediates. The total transition
enthalpy of these collagens is comparable to the transition enthalpy of the
interstitial collagens with values of 17.9 kJ/mol tripeptide units for type
XI collagen, 22.9 kJ/mol for type V (alpha 1(2) alpha 2), and 18.5 kJ/mol
for type V (alpha 1 alpha 2 alpha 3). It is shown by optical rotatory
dispersion and differential scanning calorimetry that complex transition
curves with stable intermediates exist. Type XI collagen has two main
transitions at 38.5 and 41.5 degrees C and a smaller transition at 40.1
degrees C. Type V (alpha 1(2) alpha 2) shows two main transitions at 38.2
and 42.9 degrees C and two smaller transitions at 40.1 and 41.3 degrees C.
Compared to these two collagens type V (alpha 1 alpha 2 alpha 3) unfolds at
a lower temperature with two main transitions at 36.4 and 38.1 degrees C
and two minor transitions at 40.5 and 42.9 degrees C. The intermediates
present at different temperatures are characterized by resistance to
trypsin digestion, length measurements of the resistant fragments after
rotary shadowing, and amino-terminal sequencing. One of the intermediate
peptides has been identified as belonging to the alpha 2 type V chain,
starting at position 430 and being about 380 residues long. (The residue
numbering begins with the first residue of the first amino-terminal
tripeptide unit of the main triple helix. The alpha 2(XI) chain was assumed
to be the same length as the alpha 1(XI). One intermediate was identified
from the alpha 2(XI) chain and with starting position at residue 495, and
three from the alpha 3(XI) with starting positions at residues 519, 585,
and 618.
Unfolding intermediates in the triple helix to coil transition of bovine type XI collagen and human type V collagens alpha 1(2) alpha 2 and alpha 1 alpha 2 alpha 3
Research Department, Shriners Hospital for Crippled Children, Portland, Oregon 97201.
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