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Human stefin B as a model protein to study protein folding and aggregation
Published on 2019-01-15739 Views
Folding and aggregation mechanisms are in common to most proteins. Proteins differ whether they are folded or intrinsically unfolded/disordered, however, all aggregate over partially unfolded intermed
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Presentation
Human stefin b as a model protein for folding and aggregation studies00:00
Protein science: what one should knowabout a protein03:10
Monomeric stefin B (from complex with papain)04:41
Domain-swapped dimer of stefin A in solution05:25
Crystal structure of stefin B tetramer06:54
Proline isomerization - 107:58
A very interesting arrangement of stefin b in crystal08:32
The Levinthal paradox of protein folding09:07
The problem of protein folding; 1990’10:12
Human stefin10:51
The chimeras are folded11:23
Stability and rates of folding - 111:42
Stability and rates of folding - 212:33
Kinetic parameters for the folding and unfolding of stefin A, B and chimeric mutants13:16
Aggregation14:49
Proline isomerization - 215:49
Stability: stefin B wt vs. a Pro mutant16:33
Aggregation: stefin B wt vs stefin B P74S16:56
Why we study protein folding and aggregation17:44
The hallmark of neurodegenerative diseases18:58
Protein aggregation competes with folding19:31
Special optomechanical and electro-magnetic properties20:13
Amyloif fibril formation starts from partially unfolded intermediate20:52
Stefin B fibrils protection pattern22:04
Alpha helix is flanking22:59
What model describes stefin b aggregation23:27
Thermal denaturation by CD24:25
Thermal denaturation - 125:06
Thermal denaturation - 225:14
Thermal denaturation - 325:23
Thermal denaturation - 425:40
Temporal acquisition25:50
Bi-phasic reaction of fibrillation26:51
Temperature dependence27:22
Mathematical simulation28:19
Model for the mechanism of amyloid fibril formation28:34
Introducing the problem 200230:30
From Žganec & Žerovnik31:03
Antiparallel FTIR signature31:37
Neurodegenerative disease31:50
Structural characterization of toxic oligomers32:17
Versatile Structures of α-Synuclein32:37
Structure and amyloid propensity of stefin B33:13
And stefin B pores?33:36
Transition from the tetramers and higher oligomers33:45
Calcein permeation assay34:34
Surface plasmon resonance35:16
Oligomers’ toxicity35:56
Interaction with model membranes36:26
From in vitro to cells37:02
Stefin B polyclonal antibodies37:10
Transmission electron microscopy37:45
Autophagy impairment by ROS and vs38:02
(Common) down-stream processes38:58
The proteostasis network39:57
What remains to study and why40:59
Super resolution microscopies41:21
New challenges on the border with physics42:21
Enhanced absorption42:43
Laser induced degradation43:00
Early days…43:34
Acknowledgements44:15
Other collaborators45:25