Biomaterial Database

Hydrodynamic properties and unperturbed dimensions of poly(gamma-hydroxy-L-proline) in aqueous solution. 1977

D S Clark, and W L Mattice

Intrinsic viscosities and sedimentation coefficients have been measured as a function of molecular weight for poly(gamma-hydroxy-L-proline) in water. The molecular weight range covered is 9,000-35,000. High molecular weight poly(gamma-hydroxy-L-proline) in water has the hydrodynamic behavior of a random coil immersed in a good solvent, as judged by d ln [eta]/d ln M, d ln so/d ln M, dbeta/dM, and the size of beta[= nu rho (-1)]/1/3etaM-2/3(1 - nurho)-1]. The characteristic ratio, ((r2)o/nplp2) infinity, is found to be 15.9 +/- 1.6, which is not significantly different from the result of 13.7 +/- 0.9 obtained for poly(L-proline) by Mattice and Mandelkern under the same conditions. This observation casts doubt on the importance of intrachain hydrogen bonded bridges from the hydroxyl group to a carbonyl oxygen via a water molecule. The characteristic ratios and the effects of calcium chloride on the hydroynamic properties suggest that poly(L-proline) and poly(gamma-hydroxy-L-proline) possess a similar source of flexibility which is often overlooked. Two possibilities for this flexibility are a second energy minimum about the Calpha-C' bond and cis-trans isomerization about the peptide bond.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008433	Mathematics	The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)	Mathematic
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D006860	Hydrogen Bonding	A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.	Hydrogen Bonds,Bond, Hydrogen,Hydrogen Bond
D006909	Hydroxyproline	A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.	Oxyproline,4-Hydroxyproline,cis-4-Hydroxyproline,4 Hydroxyproline,cis 4 Hydroxyproline
D013696	Temperature	The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.	Temperatures
D014867	Water	A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Hydrogen Oxide