Page 120 - Introduction to Colloid and Surface Chemistry
P. 120

110  Liquid-gas  and liquid-liquid  interfaces

        thousand-fold.  Tarry  material, dust,  etc.,  in town fogs is  responsible
        for  delay in dispersal  because  of monolayer formation.

        Surface films of proteins

        Surface  films  of  high-polymer  material,  particularly  proteins,  offer
        another  wide field of study.
          Proteins  consist  of  a  primary  structure  of  amino  acid  residues
        connected  in  a  definite  sequence  by  peptide  linkages  to  form
        polypeptide chains:
                     T              r             r

                    -CH-NH-CO-CH-NH~CO-CH-etc.


        which  may  embrace  hundreds  of  such  residues.  These  polypeptide
        chains  normally take  up  a  helical  configuration,  which is  stabilised
        mainly by hydrogen  bonding  between  spatially  adjacent  -NH-  and
         ™CO~   groups.  The  helical  polypeptide  chains  of  the  globular
        proteins  are  in  turn  folded  up  to  give  compact  and  often  nearly
        spherical  molecules.  This  configuration is  maintained by  hydrogen
        bonding,  van  der  Waals  forces  between  the  non-polar  parts,
        disulphide  cross-linking,  etc.
          Any  significant alteration  in  this  arrangement  of  the  polypeptide
        chains  without damage  to  the  primary structure  is termed  denatura-
        tion.  The  common  agents  of denaturation  are  those which would be
        expected  to  modify  hydrogen  bonds  and  other  weak  stabilising
        linkages -  e.g.  acids, alkalis, alcohol,  urea, heat, ultraviolet light and
        surface  forces.  Protein  denaturation  is accompanied  by a marked loss
        of  solubility  and  is  usually,  but  not  necessarily,  an  irreversible
        process.  Proteins  adsorb  and denature  at high-energy air-water and
        oil-water interfaces because unfolding allows the polypeptide  chains
        to  be  orientated  with most  of their  hydrophilic groups  in  the  water
        phase  and  most  of  the  hydrophobic  groups  away  from  the  water
        phase.
          If  a  small  amount  of  protein  solution  is  suitably  spread  at  the
        surface  of an  aqueous  substrate,  most of the  protein  will be  surface-
        denatured,  giving an  insoluble  monomolecular  film  before  it  has  a
        chance  to  dissolve.  The  techniques  already  described  for studying
        spread  monolayers  of  insoluble material can,  therefore,  be  used in
   115   116   117   118   119   120   121   122   123   124   125