102. Zozulya S, Stryer L (1992) Calcium—myristoyl protein switch. Proc Natl Acad Sci USA
89:11569–11573
103. Flaherty KM, Zozulya S, Stryer L, McKay DB (1993) Three-dimensional structure of
recoverin, a calcium sensor in vision. Cell 75:709–716
104. Ames JB, Ishima R, Tanaka T, Gordon JI, Stryer L, Ikura M (1997) Molecular mechanics of
calcium-myristoyl switches. Nature 389:198–202
105. Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M (1995) Sequestration of the membranetargeting myristoyl group of recoverin in the calcium-free state. Nature 376:444–447
106. Weiergräber OH, Senin II, Philippov PP, Granzin J, Koch KW (2003) Impact of n-terminal
myristoylation on the Ca
2+ -dependent conformational transition in recoverin. J Biol Chem
278:22972–22979
107. Ames JB, Porumb T, Tanaka T, Ikura M, Stryer L (1995) Amino-terminal myristoylation
includes cooperative calcium binding to recoverin. J Biol Chem 270:4526–4533
108. Ames JB, Hamasaki N, Molchanova T (2002) Structure and calcium-binding studies of a
recoverin mutant (E85Q) in an allosteric intermediate state. Biochemistry 41:5776–5787
109. Desmeules P, Penney SE, Desbat B, Salesse C (2007) Determination of the contribution of the
myristoyl group and hydrophobic amino acids of recoverin on its dynamics of binding of lipid
monolayers. Biophys J 93:2069–2082
110. Coskun U, Simons K (2011) Cell membranes: the lipid perspective. Structure 19:1543–1548
111. Simonsson L, Gunnarsson A, Wallin P, Jönsson P, Höök F (2011) Continuous lipid bilayers
derived from cell membranes for spatial molecular manipulation. J Am Chem Soc
133:14027–14032
112. Surewicz WK, Leddy JL, Mantsch HH (1990) Structure, stability and receptor interaction of
cholera toxin as studied by FTIRS. Biochemistry 29:8106–8111
113. Fishman PH (1982) Role of membrane gangliosides in the binding and action of bacterial
toxins. J Membr Biol 69:85–97
114. Kelm S (2001) Ligands for siglecs. In: Crocker PR (ed) Mammalian carbohydrate recognition
systems, vol 33. Springer, Berlin
115. Crocker PR, Kelm S (1996) Methods for studying the cellular binding properties of lectin-like
receptors. In: Herzenberg LA, Weir DM (eds) Weir’s handbook of experimental immunology.
Blackwell Science, Cambridge, pp 166.161–166.111
116. May AP, Robinson RC, Vinson M, Crocker PR, Jones EY (1998) Crystal structure of the
N-terminal domain of sialoadhesin in complex with 3
0 sialyllactose at 1.84 A resolution. Mol
Cell 1:719–728
117. Merritt EA, Sarfaty S, van der Akker F, L’Hoir C, Martial JA, Hol W (1994) Crystal structure
of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide. Protein Sci 3:166–175
118. Brunette DM, Tengvall P, Textor M, Thomsen P (2001) Titanium in medicine. Springer,
Berlin
119. Wahlgren M, Arnebrant T (1991) Protein adsorption to solid surfaces. Trends Biotechnol
9:201–208
120. Desroches MJ, Chaudhary N, Omanovic S (2007) PM-IRRAS investigation of the interaction
of serum albumin and fibrinogen with a biomedical-grade stainless steel 316LVM surface.
Biomacromolecules 8:2836–2844
121. Bella J, Berman HM (1996) Crystallographic evidence for C
α
-H
...
O¼C hydrogen bonds in a
collagen triple helix. J Mol Biol 264:734–742
122. Bella J, Eaton M, Brodsky B, Berman HM (1994) Crystal and molecular structure of a
collagen-like peptide at 1.9 A resolution. Science 266:75–81
123. Monti S, Bramanti E, Della Porta V, Onor M, D’Ulivo A, Barone V (2013) Interaction of
collagen with chlorosulphonated paraffin tanning agents: Fourier transform infrared spectroscopic analysis and molecular dynamics simulations. Phys Chem Chem Phys 15:14736–14747
124. Venugopal MG, Ramshaw JAM, Braswell E, Zhu D, Brodsky B (1994) Electrostatic interactions in collagen-like triple helical peptides. Biochemistry 33:7948–7956
References
95
89:11569–11573
103. Flaherty KM, Zozulya S, Stryer L, McKay DB (1993) Three-dimensional structure of
recoverin, a calcium sensor in vision. Cell 75:709–716
104. Ames JB, Ishima R, Tanaka T, Gordon JI, Stryer L, Ikura M (1997) Molecular mechanics of
calcium-myristoyl switches. Nature 389:198–202
105. Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M (1995) Sequestration of the membranetargeting myristoyl group of recoverin in the calcium-free state. Nature 376:444–447
106. Weiergräber OH, Senin II, Philippov PP, Granzin J, Koch KW (2003) Impact of n-terminal
myristoylation on the Ca
2+ -dependent conformational transition in recoverin. J Biol Chem
278:22972–22979
107. Ames JB, Porumb T, Tanaka T, Ikura M, Stryer L (1995) Amino-terminal myristoylation
includes cooperative calcium binding to recoverin. J Biol Chem 270:4526–4533
108. Ames JB, Hamasaki N, Molchanova T (2002) Structure and calcium-binding studies of a
recoverin mutant (E85Q) in an allosteric intermediate state. Biochemistry 41:5776–5787
109. Desmeules P, Penney SE, Desbat B, Salesse C (2007) Determination of the contribution of the
myristoyl group and hydrophobic amino acids of recoverin on its dynamics of binding of lipid
monolayers. Biophys J 93:2069–2082
110. Coskun U, Simons K (2011) Cell membranes: the lipid perspective. Structure 19:1543–1548
111. Simonsson L, Gunnarsson A, Wallin P, Jönsson P, Höök F (2011) Continuous lipid bilayers
derived from cell membranes for spatial molecular manipulation. J Am Chem Soc
133:14027–14032
112. Surewicz WK, Leddy JL, Mantsch HH (1990) Structure, stability and receptor interaction of
cholera toxin as studied by FTIRS. Biochemistry 29:8106–8111
113. Fishman PH (1982) Role of membrane gangliosides in the binding and action of bacterial
toxins. J Membr Biol 69:85–97
114. Kelm S (2001) Ligands for siglecs. In: Crocker PR (ed) Mammalian carbohydrate recognition
systems, vol 33. Springer, Berlin
115. Crocker PR, Kelm S (1996) Methods for studying the cellular binding properties of lectin-like
receptors. In: Herzenberg LA, Weir DM (eds) Weir’s handbook of experimental immunology.
Blackwell Science, Cambridge, pp 166.161–166.111
116. May AP, Robinson RC, Vinson M, Crocker PR, Jones EY (1998) Crystal structure of the
N-terminal domain of sialoadhesin in complex with 3
0 sialyllactose at 1.84 A resolution. Mol
Cell 1:719–728
117. Merritt EA, Sarfaty S, van der Akker F, L’Hoir C, Martial JA, Hol W (1994) Crystal structure
of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide. Protein Sci 3:166–175
118. Brunette DM, Tengvall P, Textor M, Thomsen P (2001) Titanium in medicine. Springer,
Berlin
119. Wahlgren M, Arnebrant T (1991) Protein adsorption to solid surfaces. Trends Biotechnol
9:201–208
120. Desroches MJ, Chaudhary N, Omanovic S (2007) PM-IRRAS investigation of the interaction
of serum albumin and fibrinogen with a biomedical-grade stainless steel 316LVM surface.
Biomacromolecules 8:2836–2844
121. Bella J, Berman HM (1996) Crystallographic evidence for C
α
-H
...
O¼C hydrogen bonds in a
collagen triple helix. J Mol Biol 264:734–742
122. Bella J, Eaton M, Brodsky B, Berman HM (1994) Crystal and molecular structure of a
collagen-like peptide at 1.9 A resolution. Science 266:75–81
123. Monti S, Bramanti E, Della Porta V, Onor M, D’Ulivo A, Barone V (2013) Interaction of
collagen with chlorosulphonated paraffin tanning agents: Fourier transform infrared spectroscopic analysis and molecular dynamics simulations. Phys Chem Chem Phys 15:14736–14747
124. Venugopal MG, Ramshaw JAM, Braswell E, Zhu D, Brodsky B (1994) Electrostatic interactions in collagen-like triple helical peptides. Biochemistry 33:7948–7956
References
95