Proteiner og proteinsstrukturer Flashcards
Hva er alle proteiner bygd opp av?
The amine and carboxylic acid functional groups found in amino acids allow them to have amphiprotic properties; a molecule (or compound) that can both donate and accept a proton.
Carboxylic acid groups (-CO2H) can be deprotonated to become negative carboxylates (-CO2- ), and α-amino groups (NH2-) can be protonated to become positive α-ammonium groups (+NH3-).
At pH values greater than the pKa of the carboxylic acid group (mean for the 20 common amino acids is about 2.2), the negative carboxylate ion predominates.
At pH values lower than the pKa of the α-ammonium group (mean for the 20 common α-amino acids is about 9.4), the nitrogen is predominantly protonated as a positively charged α-ammonium group.
Thus, at pH between 2.2 and 9.4, the predominant form adopted by α-amino acids contains a negative carboxylate and a positive α-ammonium group, so it has net zero charge.
This molecular state is known as a zwitterion, from the German Zwitter meaning hermaphrodite or hybrid.
Below pH 2.2, the predominant form will have a neutral carboxylic acid group and a positive α-ammonium ion (net charge +1), and above pH 9.4, a negative carboxylate and neutral α-amino group (net charge -1).
Amino acids also exist as zwitterions in the solid phase, and crystallize with salt-like properties unlike typical organic acids or amines.
Hva deler man aminosyrer inn i?
Hvordan foregår ioniseringen av aminosyrer og peptider?
Hvordan kan man dele inn aminosyrene i ulike klasser?
Hvilken type binding dannes mellom aminosyrer?
Hvor skjer dette?
Hva er det som gir opphav til proteinenes tredimensjonale struktur?
Hvilke protein viste man først strukturen til?
Hva kom som en overraskelse?
Hvilke kjemiske bindinger finner man i proteiner?
Hva legger man i proteiners primærstruktur?
Hvilke post-translasjonelle modifikasjoner forekommer ofte med proteiner?
Hva mener man med proteiners sekundærstruktur?
Hva er 𝛼-helikser?
Hva er 𝛽-sheets?
Hva er “loop”/”turn”-regioner?
Hva legger man i proteiners tertiærstruktur?