BEGIN:VCALENDAR
VERSION:2.0
PRODID:icalendar-ruby
CALSCALE:GREGORIAN
METHOD:PUBLISH
BEGIN:VTIMEZONE
TZID:Europe/Vienna
BEGIN:DAYLIGHT
DTSTART:20130331T030000
TZOFFSETFROM:+0100
TZOFFSETTO:+0200
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=3
TZNAME:CEST
END:DAYLIGHT
BEGIN:STANDARD
DTSTART:20121028T020000
TZOFFSETFROM:+0200
TZOFFSETTO:+0100
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=10
TZNAME:CET
END:STANDARD
END:VTIMEZONE
BEGIN:VEVENT
DTSTAMP:20260505T034726Z
UID:5004044c8e211@ist.ac.at
DTSTART:20130114T163000
DTEND:20130114T173000
DESCRIPTION:Speaker: Martina Havenith\nAbstract: The majority of chemical r
 eactions\, including many that are central to important industrial and vir
 tually all\nbiological processes\, take place in a liquid-state environmen
 t. Solvents – with water being the most\nprominent – are used to “solva
 te” molecular species ranging from industrial reagents to biological\nmol
 ecules in living cells. In the life sciences\, water is the ubiquitous sol
 vent\, sometimes even called the\n“matrix of life”. There is a vast body
  of literature that considers solvents as inert media for molecular\nproce
 sses. Transcending this traditional view\, solvents are now increasingly r
 ecognized as playing an active\nrather than a passive role in their own ri
 ght.\nRecent advances in investigative techniques and theory now make poss
 ible new approaches to probing and\ndescribing solvation on a molecular sc
 ale [1]. Just recently\, the role of water in the game of life has become\
 napparent. Our group has pioneered THz absorption spectroscopy as a new\, 
 sensitive tool for studying the\ninteractions of solutes such as saccharid
 es\, ions\, peptides or proteins with water [2\,3]. Table top THz\nsources
  allow for precise measurements of the THz absorption coefficient of aqueo
 us solutions. In addition\,\nTHz time domain spectrometers have matured to
  a technique allowing for the study changes in solvation\ndynamics in real
  time.\nThe significance of spectroscopic information in the THz frequency
  range\, especially in the case of water\nstems from the fact that the hyd
 rogen bond network of water\, which is responsible for the majority of all
 \nthe eccentricities of this otherwise simple liquid\, exhibits its resona
 nces due to collective water network\nmotions exclusively in the THz frequ
 ency range [4]. We used a combination of kinetic spectroscopy\ntechniques\
 , coupled to molecular-dynamics simulations\, to follow changes in water a
 nd protein dynamics\nas a zinc metalloprotease enzyme binds its substrate 
 [5]. The results offer perhaps a most astonishing\npicture of how finely b
 iomolecules manipulate their associated water molecules to perform their f
 unction.\nAlong the same line we could also prove that long-range protein-
 water interactions make essential\ncontributions to the antifreeze activit
 y of antifreeze proteins. These results offer a fresh view onto the role\n
 of water for biomolecular shaping and function.
LOCATION:Raiffeisen Lecture Hall\, Central Building\, ISTA
ORGANIZER:ihetzenauer@ist.ac.at
SUMMARY:Martina Havenith: The Institute Colloquium: Solvation - new answers
  to an old problem
URL:https://talks-calendar.ista.ac.at/events/472
END:VEVENT
END:VCALENDAR