BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > General
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 02-08-2013, 04:27 PM
markber's Avatar
Administrator
 
Join Date: Oct 2008
Posts: 1,538
Points: 38,561, Level: 100
Points: 38,561, Level: 100 Points: 38,561, Level: 100 Points: 38,561, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 0%
Activity: 0% Activity: 0% Activity: 0%
Last Achievements
NMR Credits: 1,550
NMR Points: 38,561
Downloads: 17
Uploads: 4
Default Why Science is broken (and how to fix it)

An interesting post from a blog that BioNMR does not aggregate:

Why Science is broken (and how to fix it)
By Morgan Giddings
1 September 2011

Bell Labs was a remarkable enterprise which, according to Wikipedia, contributed to the development of cell phones, wlan (wifi), semiconductors, compression algorithms, and many more developments that changed the way people interact with technology.

Bell Labs worked well because they brought together innovative thinkers, and let them innovate. People there didn’t have to write grant proposals, teach students, serve on committees, or work on translational research that would supposedly yield immediate “marketability”.

WLAN/wifi technology for example was first developed in 1990, yet was not widely adopted in the market for another 15 years; a “translation” time of more than a decade.

Universities were also the source of many innovations, because at their best, they also let scientists go into the lab to innovate. here were teaching duties and the occasional grant proposal that had to be written, but it wasn’t the constant treadmill of publishing, writing grants, and translation into immediate relevancy.

In a frequent scenario, university researchers would come up with some brilliant new idea and play with it for years, eventually spinning it out into a company if it continued to be promising.

But now, it seems like the whole endeavor has lost sight of the fact that all innovation and science takes time.

The current mantra in university-based biomedical research is “translation.” While translation of science into the clinic is a laudable goal, the question is, are universities and university faculty really equipped for that task?

I argue that on the whole they are just about the most poorly equipped of any entity to do this. Here’s why:

Bureaucracy. Every university I’ve encountered has piles upon piles of bureaucratic red tape, which gets worse as time goes on. This inhibits all the stuff that one needs to move rapidly in an area like translation. That includes being nimble about personnel management, budget management, and technology coordination.

Mixed missions. Universities require their faculty to play an ever larger array of roles, disallowing focus on their core strengths as innovators. Faculty must be fundraisers, promoters, managers, teachers, paper pushers, committee participants, and on top of all of that, come up with innovations that can be immediately applied.

Science by committee. The fate of grants are determined by committees. Committee-based logic is generally anathema to innovation. Innovations are always considered dangerous and risky until they become mainstream–then they are no longer innovations.

The NIH and NSF try to allow more innovation into grants, but there are ever more “coordinated” projects being funded by these agencies, where on top of the individual research is layered various committees and reviews that decide which science is good and which isn’t.

When was the last time a Nobel Prize was awarded for science planned and executed by a committee? Committees are rarely innovative. They are reactive. They are a good way of implementing checks and balances, but to try to force them to lead the way in innovation is ludicrous.

The history of computer languages makes this clear: while there have been various attempts to define languages by committee, nearly all have failed. Nikalus Wirth, creator of the PASCAL language walked out on the design committee for its predecessor Algol because it had become far too complicated.

I see the same thing happening in the “big science” projects I’ve been involved with. Ever more complexity gets added by each committee discussion, slowing down innovation and burdening faculty with ever more committee work (on top of their many other roles).

This is not the way to make science work effectively. I suspect that if it continues in this direction, eventually the whole endeavor will just collapse from its own weight. I don’t see that as a good thing.

The whole system has gone berserk, and needs to get back to basics. The basics are simple: good people doing great innovative research, and then letting companies or institutes step in to do the translational part. Specifically:

Funding must change from a short-period, project-by-project basis to one where we fund good scientists to go innovate, without having to justify to a committee exactly how their innovation may play out. It is extraordinarily rare that anyone can correctly predict how any particular innovation will impact the world, and having committees attempt to perform this function is ludicrous*. As I teach people: “nobody has a crystal ball, but they like you to pretend convincingly that you do.” The charade must stop if science is to truly progress beyond minor incremental advances.

Faculty must be allowed to focus on their core strength, which is doing innovative science, as well as teaching others how to do it. All other functions should be done by others who are trained in those things. Universities need to realize that they are shooting themselves in the foot by forcing faculty to be administrators, fund raisers, promoters, managers, and paper pushers.

We need to understand the focus on short-term translation for the fallacy that it is, and stop asking grant applicants to focus on this. Science is almost never translational in the short term. Only once ideas are of sufficient maturity that they are no longer innovative is it time to translate them into beneficial applications.

Scientists need to get a whole lot better at communicating the value of science to the world, and in the process, communicating to people that good science takes time and money, but it is a worthwhile investment that has myriad payoffs.

Science needs to start being fun again. Science should enrich and inspire people, especially younger generations. An example is space travel. For decades it inspired legions of young scientists, yet now it seems like an ever more remote pipe dream (unless you’re a multimillionare who can buy yourself a short ride into space). While focusing on fixing disease is laudable, isn’t it just as important to give younger generations something to look forward to, aside from just increasingly complex and expensive cures to diseases?

People ask me all the time why I gave up a tenured faculty job at a major research university, as if I were insane. Given what is going on in science, am I really all that insane? The system is broken, and needs fixing. I’ve figured out that it is very difficult to fix it from the inside, because then I’d be beholden to the very same organizations that require deep criticism (universities and funders). Perhaps I’ll have better luck on the outside.

And, a last note: if you still believe that science can be fun, then I hope you’ll stick with it. I know that there’s a lot of angst, and that things seem bleak. But at some point it will have to get better, and those that do stick with it will be the scientific leaders of the future


Source: Why Science is broken (and how to fix it) | Naturally Selected


.
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
NMR paper in Science
NMR paper in Science P. Neudecker, P. Robustelli, A. Cavalli, P. Walsh, P. Lundström, A. Zarrine-Afsar, S. Sharpe, M. Vendruscolo, and L.E. Kay, "Structure of an Intermediate State in Protein Folding and Aggregation," Science 336 (2012) 362-366. http://dx.doi.org/10.1126/science.1214203 Science Perspective: David Eliezer, "Visualizing Amyloid Assembly," Science 336 (2012) 308-309. http://dx.doi.org/10.1126/science.1220356https://blogger.googleusercontent.com/tracker/8663203727601106205-598889862838675141?l=nmr900.blogspot.com Read complete story on NMR900 blog
nmrlearner Journal club 0 04-20-2012 08:10 AM
[Stan NMR blog] Popular Science books
Popular Science books Books directory: A huge list of books about Science with links to Amazon. Source: Stan blog library
nmrlearner News from NMR blogs 0 03-05-2012 04:29 PM
[Stan NMR blog] Materials Science and Technology books
Materials Science and Technology books Books directory: A large list of books about Materials with links to Amazon. Source: Stan blog library
nmrlearner News from NMR blogs 0 03-05-2012 04:29 PM
[Stan NMR blog] Popular Science books
Popular Science books BOOKS LIST: A huge collection with links to Amazon. Source: Stan blog library
nmrlearner News from NMR blogs 0 03-03-2012 01:39 AM
[NMR photos] This is what science looks like. NMR
http://farm8.static.flickr.com/7028/6509774877_de23f28a1e.jpg This is what science looks like. NMR More...
nmrlearner NMR pictures 0 12-14-2011 07:14 PM
Solve Puzzles for Science | Foldit
Solve Puzzles for Science | Foldit Foldit is a revolutionary new computer game enabling the users to contribute to important scientific research. More...
nmrlearner General 0 10-26-2011 11:27 PM
[CNS Yahoo group] water refinement problem - broken structure
water refinement problem - broken structure Dear all, I'm trying to perform water refinement for the very first time (new CNS user), on an NMR ensemble of CYANA calculated protein structures but the end More...
nmrlearner News from other NMR forums 0 07-18-2011 09:41 AM
[NMR900 blog] NMR paper in Science
NMR paper in Science D.M. Korzhnev, T.L. Religa, W.Banachewicz, A.R. Fersht, L.E. Kay, "A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution", Science 329 (2010) 1312-1316. http://dx.doi.org/10.1126/science.1191723 Abstract: "Proteins can sample conformational states that are critical for function but are seldom detected directly because of their low occupancies and short lifetimes. In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, in concert with a...
nmrlearner News from NMR blogs 0 09-10-2010 12:58 PM



Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is Off
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 10:04 PM.


Map