 |
PDBsum entry 1cgd
 |
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Structure
3:893-906
(1995)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Hydration structure of a collagen peptide.
|
|
J.Bella,
B.Brodsky,
H.M.Berman.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
BACKGROUND: The collagen triple helix is a unique protein motif defined by the
supercoiling of three polypeptide chains in a polyproline II conformation. It is
a major domain of all collagen proteins and is also reported to exist in
proteins with host defense function and in several membrane proteins. The
triple-helical domain has distinctive properties. Collagen requires a high
proportion of the post-translationally modified imino acid 4-hydroxyproline and
water to stabilize its conformation and assembly. The crystal structure of a
collagen-like peptide determined to 1.85 Angstrum showed that these two features
may be related. RESULTS: A detailed analysis of the hydration structure of the
collagen-like peptide is presented. The water molecules around the carbonyl and
hydroxyprolyl groups show distinctive geometries. There are repetitive patterns
of water bridges that link oxygen atoms within a single peptide chain, between
different chains and between different triple helices. Overall, the water
molecules are organized in a semi-clathrate-like structure that surrounds and
interconnects triple helices in the crystal lattice. Hydroxyprolyl groups play a
crucial role in the assembly. CONCLUSIONS: The roles of hydroxyproline and
hydration are strongly interrelated in the structure of the collagen triple
helix. The specific, repetitive water bridges observed in this structure
buttress the triple-helical conformation. The extensively ordered hydration
structure offers a good model for the interpretation of the experimental results
on collagen stability and assembly.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
|
|
Figure 5.
Figure 5. Local hydrogen-bonding network around the four
interstitial waters, which are labeled W[1A], W[1B], W[1C] and
W[1D], shown in larger type. Figure 5. Local hydrogen-bonding
network around the four interstitial waters, which are labeled
W[1A], W[1B], W[1C] and W[1D], shown in larger type.
|
|
Figure 6.
Figure 6. Space-filling representation for the progressive
hydration of the Gly→Ala peptide as seen in the crystal
structure. The views in the top row are perpendicular to the
molecular axis, whereas those in the bottom row are parallel to
the molecular axis at the same hydration level. (a) A view of
the naked triple helix; the three peptide chains are shown in
different colors. (b) Incorporation of the first shell of water
molecules, directly hydrogen bonded to carbonyl, hydroxyl or
even amide groups on the peptide surface. (c) Incorporation of
the second shell of water molecules, hydrogen bonded to the ones
in the first shell; the filling of the superhelical groove by
solvent molecules becomes more evident. (d) Third shell of water
molecules. Figure 6. Space-filling representation for the
progressive hydration of the Gly→Ala peptide as seen in the
crystal structure. The views in the top row are perpendicular to
the molecular axis, whereas those in the bottom row are parallel
to the molecular axis at the same hydration level. (a) A view of
the naked triple helix; the three peptide chains are shown in
different colors. (b) Incorporation of the first shell of water
molecules, directly hydrogen bonded to carbonyl, hydroxyl or
even amide groups on the peptide surface. (c) Incorporation of
the second shell of water molecules, hydrogen bonded to the ones
in the first shell; the filling of the superhelical groove by
solvent molecules becomes more evident. (d) Third shell of water
molecules.
|
|
|
|
|
|
| |
The above figures are
reprinted
by permission from Cell Press:
Structure
(1995,
3,
893-906)
copyright 1995.
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
K.H.Lee,
K.Kuczera,
and
M.M.Banaszak Holl
(2011).
The severity of osteogenesis imperfecta: A comparison to the relative free energy differences of collagen model peptides.
|
| |
Biopolymers,
95,
182-193.
|
|
|
|
|
|
|
L.Vitagliano,
R.Berisio,
and
A.De Simone
(2011).
Role of hydration in collagen recognition by bacterial adhesins.
|
| |
Biophys J,
100,
2253-2261.
|
|
|
|
|
|
|
F.Xu,
L.Zhang,
R.L.Koder,
and
V.Nanda
(2010).
De novo self-assembling collagen heterotrimers using explicit positive and negative design.
|
| |
Biochemistry,
49,
2307-2316.
|
|
|
|
|
|
|
J.A.Fallas,
L.E.O'Leary,
and
J.D.Hartgerink
(2010).
Synthetic collagen mimics: self-assembly of homotrimers, heterotrimers and higher order structures.
|
| |
Chem Soc Rev,
39,
3510-3527.
|
|
|
|
|
|
|
J.Kim,
L.Gu,
L.Breschi,
L.Tjäderhane,
K.K.Choi,
D.H.Pashley,
and
F.R.Tay
(2010).
Implication of ethanol wet-bonding in hybrid layer remineralization.
|
| |
J Dent Res,
89,
575-580.
|
|
|
|
|
|
|
O.S.Rabotyagova,
P.Cebe,
and
D.L.Kaplan
(2010).
Role of polyalanine domains in beta-sheet formation in spider silk block copolymers.
|
| |
Macromol Biosci,
10,
49-59.
|
|
|
|
|
|
|
G.Shanmugam,
and
P.L.Polavarapu
(2009).
Structural transition during thermal denaturation of collagen in the solution and film states.
|
| |
Chirality,
21,
152-159.
|
|
|
|
|
|
|
J.Chen,
P.R.Callis,
and
J.King
(2009).
Mechanism of the very efficient quenching of tryptophan fluorescence in human gammaD- and gammaS-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage.
|
| |
Biochemistry,
48,
3708-3716.
|
|
|
|
|
|
|
K.E.Wyatt,
J.W.Bourne,
and
P.A.Torzilli
(2009).
Deformation-Dependent Enzyme Mechanokinetic Cleavage of Type I Collagen.
|
| |
J Biomech Eng,
131,
051004.
|
|
|
|
|
|
|
K.Okuyama,
C.Hongo,
G.Wu,
K.Mizuno,
K.Noguchi,
S.Ebisuzaki,
Y.Tanaka,
N.Nishino,
and
H.P.Bächinger
(2009).
High-resolution structures of collagen-like peptides [(Pro-Pro-Gly)(4)-Xaa-Yaa-Gly-(Pro-Pro-Gly)(4)]: Implications for triple-helix hydration and Hyp(X) puckering.
|
| |
Biopolymers,
91,
361-372.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
M.D.Shoulders,
and
R.T.Raines
(2009).
Collagen structure and stability.
|
| |
Annu Rev Biochem,
78,
929-958.
|
|
|
|
|
|
|
R.T.Raines
(2009).
Stronger and (now) longer synthetic collagen.
|
| |
Adv Exp Med Biol,
611,
xci.
|
|
|
|
|
|
|
Z.R.Yang
(2009).
Predict collagen hydroxyproline sites using support vector machines.
|
| |
J Comput Biol,
16,
691-702.
|
|
|
|
|
|
|
B.Brodsky,
G.Thiagarajan,
B.Madhan,
and
K.Kar
(2008).
Triple-helical peptides: an approach to collagen conformation, stability, and self-association.
|
| |
Biopolymers,
89,
345-353.
|
|
|
|
|
|
|
E.Hohenester,
T.Sasaki,
C.Giudici,
R.W.Farndale,
and
H.P.Bächinger
(2008).
Structural basis of sequence-specific collagen recognition by SPARC.
|
| |
Proc Natl Acad Sci U S A,
105,
18273-18277.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
F.W.Kotch,
I.A.Guzei,
and
R.T.Raines
(2008).
Stabilization of the collagen triple helix by O-methylation of hydroxyproline residues.
|
| |
J Am Chem Soc,
130,
2952-2953.
|
|
|
|
|
|
|
H.Krause,
M.Bennett,
M.Forwood,
and
J.Goh
(2008).
Biomechanical properties of raw meshes used in pelvic floor reconstruction.
|
| |
Int Urogynecol J Pelvic Floor Dysfunct,
19,
1677-1681.
|
|
|
|
|
|
|
J.S.Nyman,
Q.Ni,
D.P.Nicolella,
and
X.Wang
(2008).
Measurements of mobile and bound water by nuclear magnetic resonance correlate with mechanical properties of bone.
|
| |
Bone,
42,
193-199.
|
|
|
|
|
|
|
K.M.Ravikumar,
and
W.Hwang
(2008).
Region-specific role of water in collagen unwinding and assembly.
|
| |
Proteins,
72,
1320-1332.
|
|
|
|
|
|
|
L.C.Palmer,
C.J.Newcomb,
S.R.Kaltz,
E.D.Spoerke,
and
S.I.Stupp
(2008).
Biomimetic systems for hydroxyapatite mineralization inspired by bone and enamel.
|
| |
Chem Rev,
108,
4754-4783.
|
|
|
|
|
|
|
R.Improta,
R.Berisio,
and
L.Vitagliano
(2008).
Contribution of dipole-dipole interactions to the stability of the collagen triple helix.
|
| |
Protein Sci,
17,
955-961.
|
|
|
|
|
|
|
S.T.Khew,
Q.J.Yang,
and
Y.W.Tong
(2008).
Enzymatically crosslinked collagen-mimetic dendrimers that promote integrin-targeted cell adhesion.
|
| |
Biomaterials,
29,
3034-3045.
|
|
|
|
|
|
|
V.K.Pálfi,
and
A.Perczel
(2008).
How stable is a collagen triple helix? An ab initio study on various collagen and beta-sheet forming sequences.
|
| |
J Comput Chem,
29,
1374-1386.
|
|
|
|
|
|
|
A.Mohs,
T.Silva,
T.Yoshida,
R.Amin,
S.Lukomski,
M.Inouye,
and
B.Brodsky
(2007).
Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline.
|
| |
J Biol Chem,
282,
29757-29765.
|
|
|
|
|
|
|
D.Zhang,
U.Chippada,
and
K.Jordan
(2007).
Effect of the structural water on the mechanical properties of collagen-like microfibrils: a molecular dynamics Study.
|
| |
Ann Biomed Eng,
35,
1216-1230.
|
|
|
|
|
|
|
G.D.Fullerton,
and
A.Rahal
(2007).
Collagen structure: the molecular source of the tendon magic angle effect.
|
| |
J Magn Reson Imaging,
25,
345-361.
|
|
|
|
|
|
|
K.Kar,
and
N.Kishore
(2007).
Enhancement of thermal stability and inhibition of protein aggregation by osmolytic effect of hydroxyproline.
|
| |
Biopolymers,
87,
339-351.
|
|
|
|
|
|
|
K.Okuyama,
H.Narita,
T.Kawaguchi,
K.Noguchi,
Y.Tanaka,
and
N.Nishino
(2007).
Unique side chain conformation of a Leu residue in a triple-helical structure.
|
| |
Biopolymers,
86,
212-221.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
G.Zernia,
and
D.Huster
(2006).
Collagen dynamics in articular cartilage under osmotic pressure.
|
| |
NMR Biomed,
19,
1010-1019.
|
|
|
|
|
|
|
J.W.Ager,
R.K.Nalla,
G.Balooch,
G.Kim,
M.Pugach,
S.Habelitz,
G.W.Marshall,
J.H.Kinney,
and
R.O.Ritchie
(2006).
On the increasing fragility of human teeth with age: a deep-UV resonance Raman study.
|
| |
J Bone Miner Res,
21,
1879-1887.
|
|
|
|
|
|
|
J.W.Handgraaf,
and
F.Zerbetto
(2006).
Molecular dynamics study of onset of water gelation around the collagen triple helix.
|
| |
Proteins,
64,
711-718.
|
|
|
|
|
|
|
K.Kar,
P.Amin,
M.A.Bryan,
A.V.Persikov,
A.Mohs,
Y.H.Wang,
and
B.Brodsky
(2006).
Self-association of collagen triple helic peptides into higher order structures.
|
| |
J Biol Chem,
281,
33283-33290.
|
|
|
|
|
|
|
K.Okuyama,
G.Wu,
N.Jiravanichanun,
C.Hongo,
and
K.Noguchi
(2006).
Helical twists of collagen model peptides.
|
| |
Biopolymers,
84,
421-432.
|
|
|
|
|
|
|
M.A.Schumacher,
K.Mizuno,
and
H.P.Bächinger
(2006).
The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix.
|
| |
J Biol Chem,
281,
27566-27574.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
M.Jastrzebska,
J.Zalewska-Rejdak,
R.Wrzalik,
A.Kocot,
I.Mroz,
B.Barwinski,
A.Turek,
and
B.Cwalina
(2006).
Tannic acid-stabilized pericardium tissue: IR spectroscopy, atomic force microscopy, and dielectric spectroscopy investigations.
|
| |
J Biomed Mater Res A,
78,
148-156.
|
|
|
|
|
|
|
N.Jiravanichanun,
N.Nishino,
and
K.Okuyama
(2006).
Conformation of alloHyp in the Y position in the host-guest peptide with the pro-pro-gly sequence: implication of the destabilization of (Pro-alloHyp-Gly)10.
|
| |
Biopolymers,
81,
225-233.
|
|
|
|
|
|
|
S.Viguet-Carrin,
P.Garnero,
and
P.D.Delmas
(2006).
The role of collagen in bone strength.
|
| |
Osteoporos Int,
17,
319-336.
|
|
|
|
|
|
|
T.J.Hyde,
M.A.Bryan,
B.Brodsky,
and
J.Baum
(2006).
Sequence dependence of renucleation after a Gly mutation in model collagen peptides.
|
| |
J Biol Chem,
281,
36937-36943.
|
|
|
|
|
|
|
U.Kusebauch,
S.A.Cadamuro,
H.J.Musiol,
M.O.Lenz,
J.Wachtveitl,
L.Moroder,
and
C.Renner
(2006).
Photocontrolled folding and unfolding of a collagen triple helix.
|
| |
Angew Chem Int Ed Engl,
45,
7015-7018.
|
|
|
|
|
|
|
L.Bozec,
and
M.Horton
(2005).
Topography and mechanical properties of single molecules of type I collagen using atomic force microscopy.
|
| |
Biophys J,
88,
4223-4231.
|
|
|
|
|
|
|
M.Doi,
Y.Nishi,
S.Uchiyama,
Y.Nishiuchi,
H.Nishio,
T.Nakazawa,
T.Ohkubo,
and
Y.Kobayashi
(2005).
Collagen-like triple helix formation of synthetic (Pro-Pro-Gly)10 analogues: (4(S)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10, (4(R)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10 and (4(S)-fluoroprolyl-4(R)-fluoroprolyl-Gly)10.
|
| |
J Pept Sci,
11,
609-616.
|
|
|
|
|
|
|
M.Schumacher,
K.Mizuno,
and
H.P.Bächinger
(2005).
The crystal structure of the collagen-like polypeptide (glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)9 at 1.55 A resolution shows up-puckering of the proline ring in the Xaa position.
|
| |
J Biol Chem,
280,
20397-20403.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
S.Park,
R.J.Radmer,
T.E.Klein,
and
V.S.Pande
(2005).
A new set of molecular mechanics parameters for hydroxyproline and its use in molecular dynamics simulations of collagen-like peptides.
|
| |
J Comput Chem,
26,
1612-1616.
|
|
|
|
|
|
|
T.Kishimoto,
Y.Morihara,
M.Osanai,
S.Ogata,
M.Kamitakahara,
C.Ohtsuki,
and
M.Tanihara
(2005).
Synthesis of poly(Pro-Hyp-Gly)(n) by direct poly-condensation of (Pro-Hyp-Gly)(n), where n=1, 5, and 10, and stability of the triple-helical structure.
|
| |
Biopolymers,
79,
163-172.
|
|
|
|
|
|
|
C.Renner,
B.Saccà,
and
L.Moroder
(2004).
Synthetic heterotrimeric collagen peptides as mimics of cell adhesion sites of the basement membrane.
|
| |
Biopolymers,
76,
34-47.
|
|
|
|
|
|
|
D.Barth,
A.G.Milbradt,
C.Renner,
and
L.Moroder
(2004).
A (4R)- or a (4S)-fluoroproline residue in position Xaa of the (Xaa-Yaa-Gly) collagen repeat severely affects triple-helix formation.
|
| |
Chembiochem,
5,
79-86.
|
|
|
|
|
|
|
K.Kadler
(2004).
Matrix loading: assembly of extracellular matrix collagen fibrils during embryogenesis.
|
| |
Birth Defects Res C Embryo Today,
72,
1.
|
|
|
|
|
|
|
K.Mizuno,
T.Hayashi,
D.H.Peyton,
and
H.P.Bächinger
(2004).
Hydroxylation-induced stabilization of the collagen triple helix. Acetyl-(glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)(10)-NH(2) forms a highly stable triple helix.
|
| |
J Biol Chem,
279,
38072-38078.
|
|
|
|
|
|
|
K.Okuyama,
C.Hongo,
R.Fukushima,
G.Wu,
H.Narita,
K.Noguchi,
Y.Tanaka,
and
N.Nishino
(2004).
Crystal structures of collagen model peptides with Pro-Hyp-Gly repeating sequence at 1.26 A resolution: implications for proline ring puckering.
|
| |
Biopolymers,
76,
367-377.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
R.Berisio,
V.Granata,
L.Vitagliano,
and
A.Zagari
(2004).
Characterization of collagen-like heterotrimers: implications for triple-helix stability.
|
| |
Biopolymers,
73,
682-688.
|
|
|
|
|
|
|
I.Majsterek,
E.McAdams,
E.Adachi,
S.T.Dhume,
and
A.Fertala
(2003).
Prospects and limitations of the rational engineering of fibrillar collagens.
|
| |
Protein Sci,
12,
2063-2072.
|
|
|
|
|
|
|
J.J.Wilson,
O.Matsushita,
A.Okabe,
and
J.Sakon
(2003).
A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation.
|
| |
EMBO J,
22,
1743-1752.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
J.Stetefeld,
S.Frank,
M.Jenny,
T.Schulthess,
R.A.Kammerer,
S.Boudko,
R.Landwehr,
K.Okuyama,
and
J.Engel
(2003).
Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon.
|
| |
Structure,
11,
339-346.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
K.Mizuno,
T.Hayashi,
and
H.P.Bächinger
(2003).
Hydroxylation-induced stabilization of the collagen triple helix. Further characterization of peptides with 4(R)-hydroxyproline in the Xaa position.
|
| |
J Biol Chem,
278,
32373-32379.
|
|
|
|
|
|
|
R.Martin,
L.Waldmann,
and
D.L.Kaplan
(2003).
Supramolecular assembly of collagen triblock peptides.
|
| |
Biopolymers,
70,
435-444.
|
|
|
|
|
|
|
C.Benzi,
R.Improta,
G.Scalmani,
and
V.Barone
(2002).
Quantum mechanical study of the conformational behavior of proline and 4R-hydroxyproline dipeptide analogues in vacuum and in aqueous solution.
|
| |
J Comput Chem,
23,
341-350.
|
|
|
|
|
|
|
J.K.Rainey,
and
M.C.Goh
(2002).
A statistically derived parameterization for the collagen triple-helix.
|
| |
Protein Sci,
11,
2748-2754.
|
|
|
|
|
|
|
R.Berisio,
L.Vitagliano,
L.Mazzarella,
and
A.Zagari
(2002).
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3).
|
| |
Protein Sci,
11,
262-270.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
Z.Shi,
C.A.Olson,
G.D.Rose,
R.L.Baldwin,
and
N.R.Kallenbach
(2002).
Polyproline II structure in a sequence of seven alanine residues.
|
| |
Proc Natl Acad Sci U S A,
99,
9190-9195.
|
|
|
|
|
|
|
C.A.Miles,
and
T.V.Burjanadze
(2001).
Thermal stability of collagen fibers in ethylene glycol.
|
| |
Biophys J,
80,
1480-1486.
|
|
|
|
|
|
|
L.Vitagliano,
R.Berisio,
A.Mastrangelo,
L.Mazzarella,
and
A.Zagari
(2001).
Preferred proline puckerings in cis and trans peptide groups: implications for collagen stability.
|
| |
Protein Sci,
10,
2627-2632.
|
|
|
|
|
|
|
L.Vitagliano,
R.Berisio,
L.Mazzarella,
and
A.Zagari
(2001).
Structural bases of collagen stabilization induced by proline hydroxylation.
|
| |
Biopolymers,
58,
459-464.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
S.D.Mooney,
C.C.Huang,
P.A.Kollman,
and
T.E.Klein
(2001).
Computed free energy differences between point mutations in a collagen-like peptide.
|
| |
Biopolymers,
58,
347-353.
|
|
|
|
|
|
|
S.Perret,
C.Merle,
S.Bernocco,
P.Berland,
R.Garrone,
D.J.Hulmes,
M.Theisen,
and
F.Ruggiero
(2001).
Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation.
|
| |
J Biol Chem,
276,
43693-43698.
|
|
|
|
|
|
|
V.V.Gorbatchuk,
M.A.Ziganshin,
N.A.Mironov,
and
B.N.Solomonov
(2001).
Homotropic cooperative binding of organic solvent vapors by solid trypsin.
|
| |
Biochim Biophys Acta,
1545,
326-338.
|
|
|
|
|
|
|
A.Traore,
L.Foucat,
and
J.P.Renou
(2000).
1H-nmr study of water dynamics in hydrated collagen: transverse relaxation-time and diffusion analysis.
|
| |
Biopolymers,
53,
476-483.
|
|
|
|
|
|
|
A.V.Buevich,
Q.H.Dai,
X.Liu,
B.Brodsky,
and
J.Baum
(2000).
Site-specific NMR monitoring of cis-trans isomerization in the folding of the proline-rich collagen triple helix.
|
| |
Biochemistry,
39,
4299-4308.
|
|
|
|
|
|
|
D.E.Mechling,
and
H.P.Bachinger
(2000).
The collagen-like peptide (GER)15GPCCG forms pH-dependent covalently linked triple helical trimers.
|
| |
J Biol Chem,
275,
14532-14536.
|
|
|
|
|
|
|
J.Bella,
and
H.M.Berman
(2000).
Integrin-collagen complex: a metal-glutamate handshake.
|
| |
Structure,
8,
R121-R126.
|
|
|
|
|
|
|
J.C.Müller,
J.Ottl,
and
L.Moroder
(2000).
Heterotrimeric collagen peptides as fluorogenic collagenase substrates: synthesis, conformational properties, and enzymatic digestion.
|
| |
Biochemistry,
39,
5111-5116.
|
|
|
|
|
|
|
J.L.Lauer-Fields,
K.A.Tuzinski,
K.Shimokawa,
H.Nagase,
and
G.B.Fields
(2000).
Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases.
|
| |
J Biol Chem,
275,
13282-13290.
|
|
|
|
|
|
|
R.Berisio,
L.Vitagliano,
G.Sorrentino,
L.Carotenuto,
C.Piccolo,
L.Mazzarella,
and
A.Zagari
(2000).
Effects of microgravity on the crystal quality of a collagen-like polypeptide.
|
| |
Acta Crystallogr D Biol Crystallogr,
56,
55-61.
|
|
|
|
|
|
|
R.Berisio,
L.Vitagliano,
L.Mazzarella,
and
A.Zagari
(2000).
Crystal structure of a collagen-like polypeptide with repeating sequence Pro-Hyp-Gly at 1.4 A resolution: implications for collagen hydration.
|
| |
Biopolymers,
56,
8.
|
|
|
|
|
|
|
R.Consonni,
L.Zetta,
R.Longhi,
L.Toma,
G.Zanaboni,
and
R.Tenni
(2000).
Conformational analysis and stability of collagen peptides by CD and by 1H- and 13C-NMR spectroscopies.
|
| |
Biopolymers,
53,
99.
|
|
|
|
|
|
|
R.Valluzzi,
and
D.L.Kaplan
(2000).
Sequence-specific liquid crystallinity of collagen model peptides. I. Transmission electron microscopy studies of interfacial collagen gels.
|
| |
Biopolymers,
53,
350-362.
|
|
|
|
|
|
|
T.V.Burjanadze
(2000).
New analysis of the phylogenetic change of collagen thermostability.
|
| |
Biopolymers,
53,
523-528.
|
|
|
|
|
|
|
M.S.Ackerman,
M.Bhate,
N.Shenoy,
K.Beck,
J.A.Ramshaw,
and
B.Brodsky
(1999).
Sequence dependence of the folding of collagen-like peptides. Single amino acids affect the rate of triple-helix nucleation.
|
| |
J Biol Chem,
274,
7668-7673.
|
|
|
|
|
|
|
T.E.Klein,
and
C.C.Huang
(1999).
Computational investigations of structural changes resulting from point mutations in a collagen-like peptide.
|
| |
Biopolymers,
49,
167-183.
|
|
|
|
|
|
|
A.A.Kornyshev,
and
S.Leikin
(1998).
Symmetry laws for interaction between helical macromolecules.
|
| |
Biophys J,
75,
2513-2519.
|
|
|
|
|
|
|
G.B.Fields,
J.L.Lauer,
Y.Dori,
P.Forns,
Y.C.Yu,
and
M.Tirrell
(1998).
Protein-like molecular architecture: biomaterial applications for inducing cellular receptor binding and signal transduction.
|
| |
Biopolymers,
47,
143-151.
|
|
|
|
|
|
|
M.Gniadecka,
O.F.Nielsen,
S.Wessel,
M.Heidenheim,
D.H.Christensen,
and
H.C.Wulf
(1998).
Water and protein structure in photoaged and chronically aged skin.
|
| |
J Invest Dermatol,
111,
1129-1133.
|
|
|
|
|
|
|
N.Kuznetsova,
S.L.Chi,
and
S.Leikin
(1998).
Sugars and polyols inhibit fibrillogenesis of type I collagen by disrupting hydrogen-bonded water bridges between the helices.
|
| |
Biochemistry,
37,
11888-11895.
|
|
|
|
|
|
|
T.Sasaki,
E.Hohenester,
W.Göhring,
and
R.Timpl
(1998).
Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin.
|
| |
EMBO J,
17,
1625-1634.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
N.K.Shah,
M.Sharma,
A.Kirkpatrick,
J.A.Ramshaw,
and
B.Brodsky
(1997).
Gly-Gly-containing triplets of low stability adjacent to a type III collagen epitope.
|
| |
Biochemistry,
36,
5878-5883.
|
|
|
|
|
|
|
N.Kuznetsova,
D.C.Rau,
V.A.Parsegian,
and
S.Leikin
(1997).
Solvent hydrogen-bond network in protein self-assembly: solvation of collagen triple helices in nonaqueous solvents.
|
| |
Biophys J,
72,
353-362.
|
|
|
|
|
|
|
T.J.Franklin
(1997).
Therapeutic approaches to organ fibrosis.
|
| |
Int J Biochem Cell Biol,
29,
79-89.
|
|
|
|
|
|
|
V.C.Chan,
J.A.Ramshaw,
A.Kirkpatrick,
K.Beck,
and
B.Brodsky
(1997).
Positional preferences of ionizable residues in Gly-X-Y triplets of the collagen triple-helix.
|
| |
J Biol Chem,
272,
31441-31446.
|
|
|
|
|
|
|
Y.Feng,
G.Melacini,
and
M.Goodman
(1997).
Collagen-based structures containing the peptoid residue N-isobutylglycine (Nleu): synthesis and biophysical studies of Gly-Nleu-Pro sequences by circular dichroism and optical rotation.
|
| |
Biochemistry,
36,
8716-8724.
|
|
|
|
|
|
|
A.Rossi,
L.V.Zuccarello,
G.Zanaboni,
E.Monzani,
K.M.Dyne,
G.Cetta,
and
R.Tenni
(1996).
Type I collagen CNBr peptides: species and behavior in solution.
|
| |
Biochemistry,
35,
6048-6057.
|
|
|
|
|
|
|
J.Bella,
B.Brodsky,
and
H.M.Berman
(1996).
Disrupted collagen architecture in the crystal structure of a triple-helical peptide with a Gly-->Ala substitution.
|
| |
Connect Tissue Res,
35,
401-406.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
|
Links
