Avatar
Loaf8badge

0 Following 0 Followers
1
Like sibling children, they share common heritage (genes) and some structural homology, often appearing to play different roles in regulating biomineralization in various states of health and disease of dentin and bone (Table 2). All bind to and regulate cell differentiation via different factors [81]. They all have numerous repeat sequences, most are charged. To illustrate, we developed a PERLbas
1
Arizability can influence these forces. Together, they control the conformational entropy of the protein structure and the motilities of the protein over solid surfaces [97,98,99]. The proteins more frequently studied are large globular proteins, such as enzymes [99,100], which show some conformational changes, decreases in secondary structure or loss of three dimensional structure upon surface ad
1
Arizability can influence these forces. Together, they control the conformational entropy of the protein structure and the motilities of the protein over solid surfaces [97,98,99]. The proteins more frequently studied are large globular proteins, such as enzymes [99,100], which show some conformational changes, decreases in secondary structure or loss of three dimensional structure upon surface ad
1
Arizability can influence these forces. Together, they control the conformational entropy of the protein structure and the motilities of the protein over solid surfaces [97,98,99]. The proteins more frequently studied are large globular proteins, such as enzymes [99,100], which show some conformational changes, decreases in secondary structure or loss of three dimensional structure upon surface ad
1
Ptide absorbed to CAP was consistent with an -helix, whereas when bound to HA the structure corresponded more to a random coil [107]. We studied DPP peptides by FTIR spectroscopy and found the phosphorylated peptides in solution in the presence of HA formed -helical structures and lost their random coil characteristics [108]. Perhaps, through evolution, the most efficient strategy found by nature
1
Ptide absorbed to CAP was consistent with an -helix, whereas when bound to HA the structure corresponded more to a random coil [107]. We studied DPP peptides by FTIR spectroscopy and found the phosphorylated peptides in solution in the presence of HA formed -helical structures and lost their random coil characteristics [108]. Perhaps, through evolution, the most efficient strategy found by nature
1
Ptide absorbed to CAP was consistent with an -helix, whereas when bound to HA the structure corresponded more to a random coil [107]. We studied DPP peptides by FTIR spectroscopy and found the phosphorylated peptides in solution in the presence of HA formed -helical structures and lost their random coil characteristics [108]. Perhaps, through evolution, the most efficient strategy found by nature
1
Ptide absorbed to CAP was consistent with an -helix, whereas when bound to HA the structure corresponded more to a random coil [107]. We studied DPP peptides by FTIR spectroscopy and found the phosphorylated peptides in solution in the presence of HA formed -helical structures and lost their random coil characteristics [108]. Perhaps, through evolution, the most efficient strategy found by nature