The energy of formation of internal loops in triple‐helical collagen polypeptides

Biopolymers

Volumn 35, Issue 6, 1995, Pages 607-619

  Paterlini, M Germana ^a   Némethy, George ^b   Scheraga, Harold A ^b  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; HELIX LOOP HELIX PROTEIN;

ARTICLE; MOLECULAR INTERACTION; PROTEIN CONFORMATION; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; TRIPLE HELIX;

AMINO ACID SEQUENCE; COLLAGEN; COMPARATIVE STUDY; MACROMOLECULAR SYSTEMS; MODELS, MOLECULAR; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; THERMODYNAMICS;

EID: 0029016973     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.360350607     Document Type: Article

References (53)

1. Triple helix-coil transition of covalently bridged collagenlike peptides
2. Standard-geometry chains fitted to X-ray derived structures: Validation of the rigid-geometry approximation. I. Chain closure through a limited search of ?loop? conformations
3. Standard-geometry chains fitted to X-ray derived structures: Validation of the rigid-geometry approximation. II. Systematic searches for short loops in proteins: Applications to bovine pancreatic ribonuclease A and human lysozyme
4. Calculation of Protein Conformation by the Build-up Procedure. Application to Bovine Pancreatic Trypsin Inhibitor Using Limited Simulated Nuclear Magnetic Resonance Data