[Left-helical (PPII-PPII) type of globular protein structure: the level of the left helical type of poly-L-proline II in Kunitz trypsin inhibitor is no less than 43%. Experimental Reper spectrum of the extended left helix].
There is established that the protein trypsin inhibitor Kunitz is a globular protein of (PPII-PPII)-type. The content of poly-L-proline helix is not smaller than 43%. It has been shown by CD method that the transition from an extended left-handed helical structure to alpha-helix arises on heating till the denaturation temperatures. On this assumption the CD spectrum of poly-L-proline II type has been calculated.
Bazhulina
N P
NP
Korolev
S V
SV
Morozov
N Iu
NIu
Rogulenkova
V N
VN
Esipova
N G
NG
D002942:Circular Dichroism; D003196:Computer Graphics; D010455:Peptides / Q000032:analysis*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000737:chemistry*
D010455:Peptides; D011506:Proteins; C011083:polyproline; D014360:Trypsin Inhibitor, Kunitz Soybean
Levospiral'nyĭ (PPII-PPII) tip struktury globuliarnogo belka: v ingibitore tripsina kunitsa soderzhanie levoĭ spirali tipa poli-L-prolin II sostavliaet ne menee 43%. Eksperimental'nyĭ repernyĭspektr vytianutoĭ levoĭ spirali.