Polymorphism of collagen triple helix revealed by 19F NMR of model peptide [Pro-4(R)-hydroxyprolyl-Gly]3-[Pro-4(R)-Fluoroprolyl- Gly]-[Pro-4(R)-Hydroxyprolyl-Gly]3

Journal of Physical Chemistry B

Volumn 116, Issue 23, 2012, Pages 6908-6915

  Kawahara, Kazuki ^a   Nemoto, Nobuaki ^b   Motooka, Daisuke ^a   Nishi, Yoshinori ^c   Doi, Masamitsu ^d   Uchiyama, Susumu ^a   Nakazawa, Takashi ^e   Nishiuchi, Yuji ^f   Yoshida, Takuya ^a   Ohkubo, Tadayasu ^a   Kobayashi, Yuji ^a,c  

^a OSAKA UNIVERSITY   (Japan)

^b JEOL LTD   (Japan)

^c OSAKA MEDICAL COLLEGE   (Japan)

^d WAKAYAMA NATIONAL COLLEGE OF TECHNOLOGY   (Japan)

^e NARA WOMEN'S UNIVERSITY   (Japan)

^f Peptide Institute Inc   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MONOMERS; PEPTIDES;

COIL TRANSITION; COLLAGEN PEPTIDES; COLLAGEN TRIPLE HELIX; EXCHANGE SPECTROSCOPIES; HIGHER-ORDER STRUCTURE; MODEL PEPTIDES; NMR PROBE; PEPTIDE BONDS; SELF-ASSEMBLE; TRANSITION MECHANISM; TRIPLE HELICAL STRUCTURES; TRIPLE HELIXES; TRIPLE-HELICES; TWO-STATE MODEL;

COLLAGEN;

EID: 84862285775     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp212631q     Document Type: Article

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