Pub. Date : 2018 Jan 25
PMID : 29272129
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively. | Glutamic Acid | lactalbumin alpha | Homo sapiens |
| 2 | The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively. | Glutamic Acid | lactalbumin alpha | Homo sapiens |
| 3 | The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively. | Glutamic Acid | lactalbumin alpha | Homo sapiens |
| 4 | The present study examines the effect of a negatively charged amino acid osmolyte, glutamate (Glu), on two model proteins, ribonuclease A (RNase A) and alpha-lactalbumin (alpha-LA), which have positive and negative surface charges at pH 7, respectively. | Glutamic Acid | lactalbumin alpha | Homo sapiens |
| 5 | However, urea subverts the Glu-induced intermediate formed by alpha-LA, whereas it only slightly destabilizes in the case of RNase A which has a positive surface charge and could possess charge-charge interactions with Glu. | Glutamic Acid | lactalbumin alpha | Homo sapiens |
| 6 | The extent of stability exerted by Glu is higher for RNase A at higher temperature, whereas it provides more stability for alpha-LA at lower temperature. | Glutamic Acid | lactalbumin alpha | Homo sapiens |