Conformation is what determines a protein's unique set of functional and otherwise shapes.
A protein that has lost its native nature conformation by exposure to a destabilizing agent such as heat or detergent.
Tertiary - the protein's natural three- dimensional conformation - and Quaternary - how separately related tertiary forms coalesce.
Environment and bonding. The structure determines its function.
Juswinder Singh has written: 'Atlas of protein side-chain interactions' -- subject(s): Conformation, Protein binding, Proteins
each protein will have unique structure & conformation. thus each protein is able to do various jobs
This occurs when lipoproteins exchange their lipid and protein components with the environment.
yes a ligand is anything that can change the conformation of a receptor protein. hormones bind to proteins in the same way ligands do
Barry Robson has written: 'Introduction to proteins and protein engineering' -- subject(s): Biosynthesis, Biotechnology, Genetic intervention, Genetics, Industrial applications, Protein Conformation, Protein engineering, Proteins, Recombinant proteins
It requires energy, and a carrier protein. The large particle binds to the carrier protein on the inside of the cell. The protein then changes conformation, thus moving the particle to the outside, where it is dropped off by another conformational change in the protein.
Native Gel or the Native PAGE is the electrophoretic system in which the the proteins are run in their native conformation, that is that they are not denatured. This used when the function of the protein is important, especially enzymes, as the function of a protein is related to its native structure.
No it isn't an incomplete protein. Egg whites are just albumin protein that has been denatured by the heat of cooking. They are still whole proteins, they are just in a different conformation than their original form.