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Human stefin B as a model protein to study protein folding and aggregation
Published on Jan 15, 2019726 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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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