PMID- 2001367
OWN - NLM
STAT- MEDLINE
DCOM- 19910418
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 30
IP  - 9
DP  - 1991 Mar 5
TI  - FTIRS in H2O demonstrates that collagen monomers undergo a conformational 
      transition prior to thermal self-assembly in vitro.
PG  - 2372-7
AB  - The assembly of type I collagen molecules into native fibrils can be accomplished 
      in vitro in solutions at physiological ionic strength and pH by raising the 
      temperature above 30 degrees C. The thermal self-assembly reaction exhibits a 
      distinct lag phase. This lag phase has been proposed to be evidence for a 
      conformational transition in the monomer. Fourier transform infrared spectroscopy 
      (FTIRS) is a very sensitive probe of the H-bonded states within the triple helix. 
      The carbonyl group spectrum (amide I, 1700-1600 cm-1) has been investigated in 
      collagen/H2O solutions at 1 mg/mL under self-assembly conditions from 4 to 34 
      degrees C and, in the same range, at a higher ionic strength where self-assembly 
      does not occur. The deconvoluted spectra show three very clear bands at 
      approximately 1660, 1644, and 1630 cm-1. These bands vary in both frequency 
      maxima and relative intensity over the temperature range examined. Spectra were 
      also obtained in the amide II and III regions. Spectral changes were evident in 
      the 22-26 degrees C range, under fibril-forming conditions, which lead to the 
      hypothesis that the triple helix of the semiflexible collagen molecule is 
      actually perfected during the lag phase, facilitating nucleation and 
      intermolecular interaction. Further spectral changes after fibrils do form show 
      that the molecules are once again distorted as they are bent to fit within the 
      fibrils.
FAU - George, A
AU  - George A
AD  - Division of Oral Biology, Northwestern University, Chicago, Illinois 60611.
FAU - Veis, A
AU  - Veis A
LA  - eng
GR  - AR 13921/AR/NIAMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Macromolecular Substances)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Animals
MH  - Collagen/*chemistry
MH  - Kinetics
MH  - Macromolecular Substances
MH  - Models, Molecular
MH  - Protein Conformation
MH  - Rats
MH  - Skin/chemistry
MH  - Spectrophotometry, Infrared/methods
MH  - Thermodynamics
EDAT- 1991/03/05 00:00
MHDA- 1991/03/05 00:01
CRDT- 1991/03/05 00:00
PHST- 1991/03/05 00:00 [pubmed]
PHST- 1991/03/05 00:01 [medline]
PHST- 1991/03/05 00:00 [entrez]
AID - 10.1021/bi00223a011 [doi]
PST - ppublish
SO  - Biochemistry. 1991 Mar 5;30(9):2372-7. doi: 10.1021/bi00223a011.