1999
DOI: 10.1006/jcis.1998.5949
|View full text |Cite
|
Sign up to set email alerts
|

The Effect of Cholesterol on the Solution Structure of Proteins of Photosystem II. Protein Secondary Structure and Photosynthetic Oxygen Evolution

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3

Citation Types

0
3
0

Year Published

2007
2007
2014
2014

Publication Types

Select...
6

Relationship

0
6

Authors

Journals

citations
Cited by 6 publications
(3 citation statements)
references
References 24 publications
0
3
0
Order By: Relevance
“…In addition, amide I of bLf entrapped in liposomes had no shift in peak position compared with free bLf. Interestingly, amide II band at 1514.65 per cm disappeared or overlapped after entrapment in liposomes, which was attributed to cholesterol interaction with the polypeptide and phospholipid polar groups , allowed the insertion of bLf into the bilayer forming discoidal phospholipid–peptide assemblies . With respect to SLP, the absence of any shift in protein peak positions after encapsulation exhibited that there was no detectable structural change in bLf associated with the compositions of SLPs.…”
Section: Discussionmentioning
confidence: 99%
“…In addition, amide I of bLf entrapped in liposomes had no shift in peak position compared with free bLf. Interestingly, amide II band at 1514.65 per cm disappeared or overlapped after entrapment in liposomes, which was attributed to cholesterol interaction with the polypeptide and phospholipid polar groups , allowed the insertion of bLf into the bilayer forming discoidal phospholipid–peptide assemblies . With respect to SLP, the absence of any shift in protein peak positions after encapsulation exhibited that there was no detectable structural change in bLf associated with the compositions of SLPs.…”
Section: Discussionmentioning
confidence: 99%
“…nAChr is reportedly shown to be stabilized in its activated form by a direct action of cholesterol [19]. There are spectroscopic analyses showing that variation in cholesterol concentration can perturb protein secondary structure; this has been shown in photosystem II [67].…”
Section: Discussionmentioning
confidence: 99%
“…An alternative possibility is that because of its ability to fold and unfold KMP-11 may interact with the membrane lipid (18). There is spectroscopic evidence showing that variation in the cholesterol concentration in the membrane can perturb the protein secondary structure; this has been well studied in photosystem II of chloroplasm (8) and in the cholecystokinin receptor (24).…”
Section: Discussionmentioning
confidence: 99%