Macromolecular conformational dynamics in torsional angle space

Journal of Chemical Physics

Volumn 108, Issue 1, 1998, Pages 271-300

  He, Siqian ^a   Scheraga, Harold A ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHMS; CALCULATIONS; COMPUTER SIMULATION; CONFORMATIONS; MATHEMATICAL MODELS; MOLECULAR DYNAMICS; PROTEINS; RELAXATION PROCESSES; TENSORS;

BROWNIAN DYNAMICS; LANGEVIN EQUATION; PROTEIN FOLDING;

MACROMOLECULES;

EID: 0031678463     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.475378     Document Type: Article

References (20)

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19. That is true only when the temperature is not too high. For high enough temperature, the impact of the thermal bombardments onto the atoms on the surface of the protein will be transmitted to generate large momenta of the atoms inside the protein core and cause high temperature denaturation.
20. BT that we have chosen. Two possible explanations are given below. First, our model does not have the mechanisms employed by Nature of shielding the torsional bonds in the hydrophobic core of a protein from thermal excitations once the protein assumes a globular form. Second, our chain molecule is too small to possess a hydrophobic core in its native conformation; consequently, the native fold is relatively vulnerable (compared to real proteins) to thermal excitations (cf. part C of Sec. IV).