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Martin Gruebele
University Of Illinois Urbana-Champaign
$3,507,597
Attributed
$3,507,597
Total exposure
11
Grants
6
Lead (contact PI)
Attributed= this PI's even-split share of every grant they're on (the fair, additive number). Exposure = full size of all those grants. They are the sole PI on all grants (the two match).
Funding over time
peak $305.5K · FY2005–20$500K$375K$250K$125K$0
'05
'06
'07
'08
'09
'10
'11
'12
'13
'14
'15
'16
'17
'18
'19
'20
Funding mix
By agency
NIH$3,507,597 · 11
By mechanism
R01$3,390,975 · 2
P41$116,622 · 9
Top collaborators
No co-investigators on record.
Most similar at University Of Illinois Urbana-Champaign
Same institution · by research overlap
- Klaus J. Schulten$18,414,799
Others in their field
Top investigators on “Protein Folding”
- Ian A Wilson · Scripps Research Institute, The$84,342,359
- Andrzej Joachimiak Joachimiak · University Of Chicago$75,042,719
- John L Markley · University Of Wisconsin Madison$50,296,824
- Thomas C. Terwilliger · University Of Calif-Los Alamos Nat Lab$34,552,873
- Randal J. Kaufman · Indiana University Indianapolis$32,925,928
- John R Boisseau · University Of Texas At Austin$31,886,920
Research focus
Protein FoldingProteinsKineticsSimulationSiteComplexStructureEquilibriumLambda RepressorMutantMolecular DynamicsProtein AggregationThermodynamicsTemperatureIllinoisResearch StudyBiological ModelsCoupledRelaxationRna BindingBinding ProteinsAmyloidComplementComputers
Grant awards (23)
Protein domains interacting with crowders, RNA and other protein domains$291,889
R01 · FY2020 · GM · contact PI
Protein domains interacting with crowders, RNA and other protein domains$291,369
R01 · FY2019 · GM · contact PI
Protein domains interacting with crowders, RNA and other protein domains$291,369
R01 · FY2018 · GM · contact PI
Protein domains interacting with crowders, RNA and other protein domains$292,410
R01 · FY2017 · GM · contact PI
Fast model systems for misfolding, binding and aggregation$278,675
R01 · FY2016 · GM · contact PI
Fast model systems for misfolding, binding and aggregation$276,362
R01 · FY2015 · GM · contact PI
Fast model systems for misfolding, binding and aggregation$269,725
R01 · FY2014 · GM · contact PI
Fast model systems for misfolding, binding and aggregation$305,541
R01 · FY2013 · GM · contact PI
Protein refolding and transient aggregate formation studied by very fast pressure$260,175
R01 · FY2012 · GM · contact PI
Protein refolding and transient aggregate formation studied by very fast pressure$243,959
R01 · FY2011 · GM · contact PI
LONG TIMESCALE MOLECULAR DYNAMICS SIMULATION OF PROTEIN FOLDING$1,094
P41 · FY2011 · RR · contact PI
Protein refolding and transient aggregate formation studied by very fast pressure$251,868
R01 · FY2010 · GM · contact PI
SAXS-DETECTED DYNAMICS OF FAST-FOLDING PROTEINS$25,364
P41 · FY2008 · RR · contact PI
SAXS-DETECTED DYNAMICS OF FAST-FOLDING PROTEINS$35,325
P41 · FY2007 · RR · contact PI
MEASURING COLLAPSE KINETICS OF LAMBDA REPRESSOR$13,285
P41 · FY2006 · RR · contact PI
EQUILIBRIUM FLUORESCENCE MEASUREMNTS OF MEMBRANE PEPTIDES$5,925
P41 · FY2006 · RR · contact PI
MEASURING COLLAPSE KINETICS OF LAMBDA REPRESSOR$13,286
P41 · FY2005 · RR
EQUILIBRIUM FLUORESCENCE MEASUREMNTS OF MEMBRANE PEPTIDES$5,078
P41 · FY2005 · RR
FLUORESCENCE OF LIPOSOMES AND LIPID-BINDING PEPTIDES$13,529
P41 · FY2004 · RR
EQUILIBRIUM FLUORESCENCE MEASUREMENTS OF MEMBRANE PEPTID$3,332
P41 · FY2004 · RR
(APOMYOGLOBIN)/SYNTHETIC HELICAL PEPTIDES$404
P41 · FY2004 · RR
SUBMILLISECOND LASER T JUMP INDUCED PROTEIN FOLDING$153,128
R01 · FY2001 · GM
SUBMILLISECOND LASER T JUMP INDUCED PROTEIN FOLDING$184,505
R01 · FY2000 · GM