Differential scanning calorimetry study of the hydrophobic hydration of the elastin-based polypentapeptide, poly(VPGVG), from deficiency to excess of water.
The polypentapeptide of elastin, poly(VPGVG), has become an interesting model polypeptide in understanding the mechanism of protein folding and assembly. Due to its simple amino acid composition and the predominance of apolar side chains, this polymer shows strong hydrophobic-hydration phenomena. This paper explores, by calorimetric methods, the nature and structure of the clathrate-like arrangements that take place, surrounding the apolar side chains of the polymer. The performance of these methods, especially differential scanning calorimetry, has a well-gained reputation. In this work, the development of the clathrate-like structures around this model polymer has been followed from water deficiency to water-excess states. Two main conclusions have been obtained from the data obtained. First, there is an upper limit of about 170 water molecules per pentamer as the number of water molecules required to form all the possible clathrate-like structures. Second, these structures exist as an inhomogeneous population with energies spreading in a significantly broad range, which is likely related to differences in geometrical parameters (bond lengths and angles) of the clathrate structure.
Rodríguez-Cabello
J C
JC
Dpto. Física de la Materia Condensada, E.T.S.I.I./Universidad de Valladolid, Paseo del Cauce s/n, 47005 Valladolid, Spain. cabello@wfisic.eis.uva.es
Alonso
M
M
Pérez
T
T
Herguedas
M M
MM
D000595:Amino Acid Sequence; D002152:Calorimetry, Differential Scanning; D004549:Elastin / Q000737:chemistry*; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D010455:Peptides; D014867:Water; C058088:valyl-prolyl-glycyl-valyl-glycine polypeptide; D004549:Elastin