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secondary structures formation is avoided by using short sequence peptides. Derivatization of amino acids is necessary to ease its partition into a C18 bonded phase. Another scale had been developed in 1971 and used peptide retention on hydrophilic gel. 1-butanol and pyridine were used as the mobile phase in this particular scale and glycine was used as the reference value. Pliska and his coworkers used thin layer chromatography to relate mobility values of free amino acids to their hydrophobicities. About a decade ago, another hydrophilicity scale was published, this scale used normal phase liquid chromatography and showed the retention of 121 peptides on an amide-80 column. The absolute values and relative rankings of hydrophobicity determined by chromatographic methods can be affected by a number of parameters. These parameters include the silica surface area and pore diameter, the choice and pH of aqueous buffer, temperature and the bonding density of stationary phase chains.
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of various dielectric medium generated by arrangement of different amino acids. Hence, different parts of the protein structure most likely would behave as solvents with different dielectric values. For simplicity, each protein structure was considered as an immiscible mixture of two solvents, protein interior and protein exterior. The local environment around individual amino acid (termed as "micro-environment") was computed for both protein interior and protein exterior. The ratio gives the relative hydrophobicity scale for individual amino acids. Computation was trained on high resolution protein crystal structures. This quantitative descriptor for microenvironment was derived from the
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tension values for the naturally occurring 20 amino acids in NaCl solution. The main drawbacks of surface tension measurements is that the broken hydrogen bonds and the neutralized charged groups remain at the solution air interface. Another physical property method involve measuring the solvation free energy. The solvation free energy is estimated as a product of an accessibility of an atom to the solvent and an atomic solvation parameter. Results indicate the solvation free energy lowers by an average of 1 Kcal/residue upon folding.
201:
on a bioinformatic survey of 5526 high-resolution structures from the
Protein Data Bank. This differential scale has two comparative advantages: (1) it is especially useful for treating changes in water-protein interactions that are too small to be accessible to conventional force-field calculations, and (2) for homologous structures, it can yield correlations with changes in properties from mutations in the amino acid sequences alone, without determining corresponding structural changes, either in vitro or in vivo.
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making it difficult to obtain pure hydrophobicity scale. Nozaki and
Tanford proposed the first major hydrophobicity scale for nine amino acids. Ethanol and dioxane are used as the organic solvents and the free energy of transfer of each amino acid was calculated. Non liquid phases can also be used with partitioning methods such as micellar phases and vapor phases. Two scales have been developed using micellar phases. Fendler et al. measured the partitioning of 14 radiolabeled amino acids using
152:
tendency for a residue to be found inside of a protein rather than on its surface. Since cysteine forms disulfide bonds that must occur inside a globular structure, cysteine is ranked as the most hydrophobic. The first and third scales are derived from the physiochemical properties of the amino acid side chains. These scales result mainly from inspection of the amino acid structures. Biswas et al., divided the scales based on the method used to obtain the scale into five different categories.
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the increased stability is directly proportional to increase in hydrophobicity up to a certain size limit. The main disadvantage of site-directed mutagenesis method is that not all the 20 naturally occurring amino acids can substitute a single residue in a protein. Moreover, these methods have cost problems and is useful only for measuring protein stability.
169:. Also, amino acid side chain affinity for water was measured using vapor phases. Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden. Aqueous and
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Most of the existing hydrophobicity scales are derived from the properties of amino acids in their free forms or as a part of a short peptide. Bandyopadhyay-Mehler hydrophobicity scale was based on partitioning of amino acids in the context of protein structure. Protein structure is a complex mosaic
239:
methods are based on the measurement of different physical properties. Examples include, partial molar heat capacity, transition temperature and surface tension. Physical methods are easy to use and flexible in terms of solute. The most popular hydrophobicity scale was developed by measuring surface
218:
This method use DNA recombinant technology and it gives an actual measurement of protein stability. In his detailed site-directed mutagenesis studies, Utani and his coworkers substituted 19 amino acids at Trp49 of the tryptophan synthase and he measured the free energy of unfolding. They found that
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for the corresponding types of atoms. A differential solvent accessible surface area hydrophobicity scale based on proteins as compacted networks near a critical point, due to self-organization by evolution, was constructed based on asymptotic power-law (self-similar) behavior. This scale is based
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The most common method of measuring amino acid hydrophobicity is partitioning between two immiscible liquid phases. Different organic solvents are most widely used to mimic the protein interior. However, organic solvents are slightly miscible with water and the characteristics of both phases change
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of a hard-sphere solute with respect to that in the bulk exhibits a linear dependence on cosine value of contact angle. Based on the computed excess chemical potentials of the purely repulsive methane-sized Weeks–Chandler–Andersen solute with respect to that in the bulk, the extrapolated values of
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Palliser and Parry have examined about 100 scales and found that they can use them for locating B-strands on the surface of proteins. Hydrophobicity scales were also used to predict the preservation of the genetic code. Trinquier observed a new order of the bases that better reflect the conserved
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team recently devised a computational approach that can relate the molecular hydrophobicity scale of amino-acid chains to the contact angle of water nanodroplet. The team constructed planar networks composed of unified amino-acid side chains with native structure of the beta-sheet protein. Using
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The
Stephen H. White website provides an example of whole residue hydrophobicity scales showing the free energy of transfer ΔG(kcal/mol) from water to POPC interface and to n-octanol. These two scales are then used together to make Whole residue hydropathy plots. The hydropathy plot constructed
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of the system. In terms of thermodynamics, the hydrophobic effect is the free energy change of water surrounding a solute. A positive free energy change of the surrounding solvent indicates hydrophobicity, whereas a negative free energy change implies hydrophilicity. In this way, the hydrophobic
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The Wimley–White whole residue hydrophobicity scales are significant for two reasons. First, they include the contributions of the peptide bonds as well as the sidechains, providing absolute values. Second, they are based on direct, experimentally determined values for transfer free energies of
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as the most hydrophobic residue, unlike the other two scales. This difference is due to the different methods used to measure hydrophobicity. The method used to obtain the Janin and Rose et al. scales was to examine proteins with known 3-D structures and define the hydrophobic character as the
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phases were used in the development of a novel partitioning scale. Partitioning methods have many drawbacks. First, it is difficult to mimic the protein interior. In addition, the role of self solvation makes using free amino acids very difficult. Moreover, hydrogen bonds that are lost in the
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Reversed phase liquid chromatography (RPLC) is the most important chromatographic method for measuring solute hydrophobicity. The non polar stationary phase mimics biological membranes. Peptide usage has many advantages because partition is not extended by the terminal charges in RPLC. Also,
99:, cannot accept or donate hydrogen bonds to water. Introduction of hexane into water causes disruption of the hydrogen bonding network between water molecules. The hydrogen bonds are partially reconstructed by building a water "cage" around the hexane molecule, similar to that in
678:, (known as Rekker's Fragmental Constants) widely used for pharmacophores. This scale well correlate with the existing methods, based on partitioning and free energy computations. Advantage of this scale is it is more realistic, as it is in the context of real protein structures.
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Zaslavsky, B. Yu.; Mestechkina, N.M.; Miheeva, L.M.; Rogozhin, S.V. (1982). "Measurement of relative hydrophobicity of amino acid side-chains by partition in an aqueous two-phase polymeric system: Hydrophobicity scale for non-polar and ionogenic side-chains".
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shows favorable peaks on the absolute scale that correspond to the known TM helices. Thus, the whole residue hydropathy plots illustrate why transmembrane segments prefer a transmembrane location rather than a surface one.
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character of the genetic code. They believed new ordering of the bases was uracil-guanine-cystosine-adenine (UGCA) better reflected the conserved character of the genetic code compared to the commonly seen ordering UCAG.
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Plass, Monika; Valko, Klara; Abraham, Michael H (1998). "Determination of solute descriptors of tripeptide derivatives based on high-throughput gradient high-performance liquid chromatography retention data".
1711:
Hodges, Robert S.; Zhu, Bing-Yan; Zhou, Nian E.; Mant, Colin T. (1994). "Reversed-phase liquid chromatography as a useful probe of hydrophobic interactions involved in protein folding and protein stability".
1424:
Sharp, Kim A.; Nicholls, Anthony; Friedman, Richard; Honig, Barry (1991-10-08). "Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models".
1790:
Pliška, Vladimir; Schmidt, Manfred; Fauchère, Jean-Luc (1981). "Partition coefficients of amino acids and hydrophobic parameters π of their side-chains as measured by thin-layer chromatography".
1389:
Leodidis, Epaminondas B.; Hatton, T. Alan. (1990). "Amino acids in AOT reversed micelles. 2. The hydrophobic effect and hydrogen bonding as driving forces for interfacial solubilization".
1863:"Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit"
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cosine value of contact angle are calculated(ccHydrophobicity), which can be used to quantify the hydrophobicity of amino acid side chains with complete wetting behaviors.
2168:
Wimley, William C.; Creamer, Trevor P.; White, Stephen H. (1996). "Solvation
Energies of Amino Acid Side Chains and Backbone in a Family of Host−Guest Pentapeptides".
2030:
Palliser, Christopher C.; Parry, David A. D. (2000). "Quantitative comparison of the ability of hydropathy scales to recognize surface ?-strands in proteins".
54:. When consecutively measuring amino acids of a protein, changes in value indicate attraction of specific protein regions towards the hydrophobic region inside
2265:"Characterizing hydrophobicity of amino acid side chains in a protein environment via measuring contact angle of a water nanodroplet on planar peptide network"
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Bandyopadhyay, D., Mehler, E.L. (2008). "Quantitative expression of protein heterogeneity: Response of amino acid side chains to their local environment".
136:
A table comparing four different scales for the hydrophobicity of an amino acid residue in a protein with the most hydrophobic amino acids on the top
1119:
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Biswas, Kallol M.; DeVido, Daniel R.; Dorsey, John G. (2003). "Evaluation of methods for measuring amino acid hydrophobicities and interactions".
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One for the transfer of unfolded chains from water to the bilayer interface (referred to as the Wimley–White interfacial hydrophobicity scale).
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molecular dynamics simulation, the team is able to measure the contact angle of water nanodroplet on the planar networks (caHydrophobicity).
691:
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Rose, G.; Geselowitz, A.; Lesser, G.; Lee, R.; Zehfus, M. (1985-08-30). "Hydrophobicity of amino acid residues in globular proteins".
2117:
Wimley, William C.; White, Stephen H. (1996). "Experimentally determined hydrophobicity scale for proteins at membrane interfaces".
1928:
Bull, Henry B.; Breese, Keith (1974). "Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues".
1278:
Wolfenden, R.; Andersson, L.; Cullis, P. M.; Southgate, C. C. B. (1981). "Affinities of amino acid side chains for solvent water".
61:
The hydrophobic or hydrophilic character of a compound or amino acid is its hydropathic character, hydropathicity, or hydropathy.
2043:
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Whole-residue octanol-scale hydropathy plot for the L-subunit of the photosynthetic reaction center of
Rhodobacter sphaeroides.
197:
702:
The MD simulation system and the structure of artificial beta-folding 2D peptide network composed of unified R-side chains.
1330:
Fendler, Janos H.; Nome, Faruk; Nagyvary, Joseph (1975). "Compartmentalization of amino acids in surfactant aggregates".
675:
766:
Kyte, Jack; Doolittle, Russell F. (May 1982). "A simple method for displaying the hydropathic character of a protein".
17:
1755:
Aboderin, Akintola A. (1971). "An empirical hydrophobicity scale for α-amino-acids and some of its applications".
895:
Charton, Marvin; Charton, Barbara I. (1982). "The structural dependence of amino acid hydrophobicity parameters".
189:
147:
There are clear differences between the four scales shown in the table. Both the second and fourth scales place
2410:
2324:"Characterizing hydrophobicity of interfaces by using cavity formation, solute binding, and water correlations"
719:
2220:
White, Stephen H.; Wimley, William C. (1999). "MEMBRANE PROTEIN FOLDING AND STABILITY: Physical
Principles".
276:
One for the transfer of unfolded chains into octanol, which is relevant to the hydrocarbon core of a bilayer.
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are the amino acids located in that region of the protein. These scales are commonly used to predict the
2263:
Zhu, Chongqin; Gao, Yurui; Li, Hui; Meng, Sheng; Li, Lei; Francisco, Joseph S; Zeng, Xiao Cheng (2016).
1609:
Moret, M. A.; Zebende, G. F. (2007-01-19). "Amino acid hydrophobicity and accessible surface area".
714:
ability) of a flat surface (e.g., a counter top in kitchen or a cooking pan) can be measured by the
780:
1971:
Eisenberg, David; McLachlan, Andrew D. (1986). "Solvation energy in protein folding and binding".
1030:
Rose, G D; Wolfenden, R (1993). "Hydrogen
Bonding, Hydrophobicity, Packing, and Protein Folding".
698:
1660:
Phillips, J. C. (2009-11-20). "Scaling and self-organized criticality in proteins: Lysozymec".
775:
162:
686:
1113:
87:
to exclude non-polar molecules. The effect originates from the disruption of highly dynamic
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1980:
1874:
1669:
1618:
1339:
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1174:
904:
740:
107:) is strongly restricted. This leads to significant losses in translational and rotational
47:
2385:
2096:
8:
2405:
1512:
Ben-Naim, A. (1990-02-15). "Solvent effects on protein association and protein folding".
995:
Eisenberg D (July 1984). "Three-dimensional structure of membrane and surface proteins".
2280:
1984:
1878:
1673:
1622:
1343:
1237:
1178:
1043:
1008:
908:
2350:
2323:
2299:
2264:
2150:
2063:
2012:
1566:
Chothia, Cyrus (1976). "The nature of the accessible and buried surfaces in proteins".
1545:
1371:
1206:
1101:
972:
947:
727:
183:
95:
do not cause the hydrophobic effect. However, a pure hydrocarbon molecule, for example
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2016:
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transfer to organic solvents are not reformed but often in the interior of protein.
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132:
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formed at lower temperatures. The mobility of water molecules in the "cage" (or
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35:
31:
91:
between molecules of liquid water. Polar chemical groups, such as OH group in
2399:
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2189:
2138:
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1733:
1689:
1638:
1587:
1533:
1489:
1445:
1410:
1359:
1299:
1253:
1232:(4716). American Association for the Advancement of Science (AAAS): 834–838.
1194:
1051:
963:
924:
864:
715:
88:
75:
55:
2375:
2340:
2289:
1887:
1245:
2380:
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2059:
1697:
1646:
1097:
981:
872:
2197:
2146:
2008:
1957:
1914:
1741:
1541:
1525:
1453:
1367:
1307:
1261:
1059:
1016:
932:
797:
1595:
1202:
707:
227:
193:
43:
2130:
1437:
1402:
1291:
84:
2044:
10.1002/1097-0134(20010201)42:2<243::aid-prot120>3.0.co;2-b
1351:
1165:
Janin, Joël (1979). "Surface and inside volumes in globular proteins".
1089:
296:
39:
2210:
White SH. & Wimley WC (1998). Biochim. Biophys. Acta 1376:339-352.
2181:
668:
1992:
1186:
711:
140:
A number of different hydrophobicity scales have been developed. The
1133:
726:
On the other hand, previous studies show that the minimum of excess
681:
1466:
260:
166:
148:
117:
92:
2381:
NetSurfP - Secondary
Structure and Surface accessibility predictor
1873:(13). Proceedings of the National Academy of Sciences: 4441–4444.
1861:
Yutani, K.; Ogasahara, K.; Tsujita, T.; Sugino, Y. (1987-07-01).
1277:
694:
on the artificial beta-sheets with various amino acid side chains
170:
121:
111:
of water molecules and makes the process unfavorable in terms of
108:
192:
for amino acid residues in the expended polypeptide chain or in
141:
96:
188:
Hydrophobicity scales can also be obtained by calculating the
945:
144:
Protscale website lists a total of 22 hydrophobicity scales.
2080:
G . Trinquier, Y.-H. Sanejouand, Protein Eng. 11 (1998) 153.
1860:
269:
Two whole-residue hydrophobicity scales have been measured:
127:
64:
2376:
ProtScale (web-based tool for calculating hydropathy plots)
1979:(6050). Springer Science and Business Media LLC: 199–203.
1423:
1173:(5696). Springer Science and Business Media LLC: 491–492.
946:
Schauperl, M; Podewitz, M; Waldner, BJ; Liedl, KR (2016).
116:
effect not only can be localized but also decomposed into
1502:
S . Damadoran, K.B. Song, J. Biol. Chem. 261 (1986) 7220.
810:
Tanford, C., The hydrophobic effect(New York:Wiley.1980).
2125:(10). Springer Science and Business Media LLC: 842–848.
948:"Enthalpic and Entropic Contributions to Hydrophobicity"
1338:(3). Springer Science and Business Media LLC: 215–232.
1320:
Y . Nozaki, C. Tanford, J. Biol. Chem. 246 (1971) 2211.
1223:
2222:
Annual Review of
Biophysics and Biomolecular Structure
1032:
Annual Review of
Biophysics and Biomolecular Structure
2321:
1789:
1867:
Proceedings of the National Academy of Sciences USA
1329:
669:
Bandyopadhyay-Mehler protein structure based scales
2176:(16). American Chemical Society (ACS): 5109–5124.
2167:
1970:
1432:(40). American Chemical Society (ACS): 9686–9697.
1397:(16). American Chemical Society (ACS): 6411–6420.
842:
177:
83:The hydrophobic effect represents the tendency of
2097:"Experimentally Determined Hydrophobicity Scales"
1824:
1710:
1078:Proteins: Structure, Function, and Bioinformatics
1075:
682:Scale based on contact angle of water nanodroplet
2397:
1273:
1271:
261:Wimley–White whole residue hydrophobicity scales
231:Wimley-White whole-residue hydrophobicity scales
79:Hydrogen bonds between molecules of liquid water
42:residues. The more positive the value, the more
2328:Proceedings of the National Academy of Sciences
2269:Proceedings of the National Academy of Sciences
1286:(4). American Chemical Society (ACS): 849–855.
804:
2322:Godawat, R; Jamadagni, S. N; Garde, S (2009).
1668:(5). American Physical Society (APS): 051916.
1617:(1). American Physical Society (APS): 011920.
1388:
894:
2029:
1268:
1029:
885:W . Kauzmann, Adv. Protein Chem. 14 (1959) 1.
765:
2262:
1608:
1118:: CS1 maint: multiple names: authors list (
939:
222:
213:
2219:
2116:
2032:Proteins: Structure, Function, and Genetics
1071:
1069:
994:
838:
836:
761:
759:
757:
755:
1927:
1561:
1559:
952:Journal of Chemical Theory and Computation
834:
832:
830:
828:
826:
824:
822:
820:
818:
816:
204:
2349:
2339:
2298:
2288:
2119:Nature Structural & Molecular Biology
2090:
2088:
2086:
1904:
1886:
971:
779:
196:and multiplying the surface areas by the
128:Types of amino acid hydrophobicity scales
65:Hydrophobicity and the hydrophobic effect
1754:
1659:
1511:
1066:
752:
697:
685:
242:
226:
131:
74:
1930:Archives of Biochemistry and Biophysics
1565:
1556:
813:
235:The hydrophobicity scales developed by
155:
14:
2398:
2083:
251:
2094:
1757:International Journal of Biochemistry
1164:
30:are values that define the relative
1044:10.1146/annurev.bb.22.060193.002121
1009:10.1146/annurev.bi.53.070184.003115
676:octanol-water partition coefficient
24:
2386:Whole residue hydrophobicity scale
2099:. University of California, Irvine
25:
2422:
2369:
1391:The Journal of Physical Chemistry
2234:10.1146/annurev.biophys.28.1.319
190:solvent accessible surface areas
2315:
2256:
2213:
2204:
2161:
2110:
2074:
2023:
1964:
1921:
1854:
1818:
1783:
1748:
1704:
1653:
1602:
1505:
1496:
1460:
1417:
1382:
1323:
1314:
1217:
1158:
1144:
1126:
178:Accessible surface area methods
2228:(1). Annual Reviews: 319–365.
1332:Journal of Molecular Evolution
1038:(1). Annual Reviews: 381–415.
1023:
988:
897:Journal of Theoretical Biology
888:
879:
720:University of Nebraska-Lincoln
198:empirical solvation parameters
13:
1:
2095:White, Stephen (2006-06-29).
1840:10.1016/s0021-9673(97)01215-6
1804:10.1016/s0021-9673(00)82337-7
1482:10.1016/s0021-9673(01)84003-6
857:10.1016/s0021-9673(03)00182-1
851:(1–2). Elsevier BV: 637–655.
746:
1942:10.1016/0003-9861(74)90352-x
1769:10.1016/0020-711x(71)90023-1
1763:(11). Elsevier BV: 537–544.
1726:10.1016/0021-9673(94)80452-4
1580:10.1016/0022-2836(76)90191-1
1568:Journal of Molecular Biology
917:10.1016/0022-5193(82)90191-6
790:10.1016/0022-2836(82)90515-0
768:Journal of Molecular Biology
7:
1936:(2). Elsevier BV: 665–670.
1834:(1–2). Elsevier BV: 51–60.
1828:Journal of Chromatography A
1792:Journal of Chromatography A
1714:Journal of Chromatography A
1470:Journal of Chromatography A
903:(4). Elsevier BV: 629–644.
845:Journal of Chromatography A
734:
48:transmembrane alpha-helices
10:
2427:
1682:10.1103/physreve.80.051916
1631:10.1103/physreve.75.011920
774:(1). Elsevier BV: 105–32.
690:Contact angles of a water
181:
68:
2391:Membrane protein explorer
1476:(1). Elsevier BV: 21–28.
710:, the hydrophobicity (or
223:Physical property methods
214:Site-directed mutagenesis
1720:(1). Elsevier BV: 3–15.
1574:(1). Elsevier BV: 1–12.
964:10.1021/acs.jctc.6b00422
2341:10.1073/pnas.0902778106
2290:10.1073/pnas.1616138113
1888:10.1073/pnas.84.13.4441
1246:10.1126/science.4023714
1152:"Hydrophobicity Scales"
205:Chromatographic methods
1798:. Elsevier BV: 79–92.
703:
695:
248:
232:
163:sodium dodecyl sulfate
137:
80:
2411:Intermolecular forces
2038:(2). Wiley: 243–255.
1526:10.1002/bip.360290312
1520:(3). Wiley: 567–596.
701:
689:
325:Octanol − interface,
246:
230:
135:
78:
28:Hydrophobicity scales
1134:"Expasy - ProtScale"
741:Hydrophobic mismatch
718:of water droplet. A
156:Partitioning methods
2334:(36): 15119–15124.
2281:2016PNAS..11312946Z
2275:(46): 12946–12951.
2131:10.1038/nsb1096-842
1985:1986Natur.319..199E
1879:1987PNAS...84.4441Y
1674:2009PhRvE..80e1916P
1623:2007PhRvE..75a1920M
1438:10.1021/bi00104a017
1403:10.1021/j100379a047
1344:1975JMolE...6..215F
1292:10.1021/bi00507a030
1238:1985Sci...229..834R
1179:1979Natur.277..491J
909:1982JThBi..99..629C
252:Recent applications
1352:10.1007/bf01732358
1090:10.1002/prot.21958
997:Annu. Rev. Biochem
728:chemical potential
704:
696:
249:
233:
184:Implicit solvation
138:
101:clathrate hydrates
81:
71:Hydrophobic effect
2182:10.1021/bi9600153
1662:Physical Review E
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52:membrane proteins
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21:
18:Hydropathy index
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105:solvation shell
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1138:web.expasy.org
1125:
1084:(2): 646–659.
1065:
1022:
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958:(9): 4600–10.
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77:
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62:
59:
57:
56:lipid bilayer
53:
49:
45:
41:
37:
33:
29:
19:
2331:
2327:
2317:
2272:
2268:
2258:
2225:
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2215:
2206:
2173:
2170:Biochemistry
2169:
2163:
2122:
2118:
2112:
2101:. Retrieved
2076:
2035:
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2025:
1976:
1972:
1966:
1933:
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1429:
1426:Biochemistry
1425:
1419:
1394:
1390:
1384:
1335:
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1325:
1316:
1283:
1280:Biochemistry
1279:
1229:
1225:
1219:
1170:
1166:
1160:
1146:
1137:
1128:
1114:cite journal
1081:
1077:
1035:
1031:
1025:
1000:
996:
990:
955:
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335:
328:
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304:
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268:
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234:
217:
208:
187:
159:
146:
139:
82:
60:
27:
26:
1514:Biopolymers
1003:: 595–623.
708:engineering
692:nanodroplet
322:(kcal/mol)
310:(kcal/mol)
194:alpha-helix
113:free energy
44:hydrophobic
2406:Biophysics
2400:Categories
2103:2009-06-12
747:References
297:Amino acid
40:amino acid
2242:1056-8700
2190:0006-2960
2139:1545-9993
2052:0887-3585
2001:0028-0836
1950:0003-9861
1897:0027-8424
1848:0021-9673
1812:0021-9673
1777:0020-711X
1734:0021-9673
1690:1539-3755
1639:1539-3755
1588:0022-2836
1534:0006-3525
1490:0021-9673
1446:0006-2960
1411:0022-3654
1360:0022-2844
1300:0006-2960
1254:0036-8075
1195:0028-0836
1052:1056-8700
925:0022-5193
865:0021-9673
776:CiteSeerX
712:dewetting
118:enthalpic
2360:19706896
2309:27803319
2250:10410805
2068:23839522
2060:11119649
2017:21867582
1698:20365015
1647:17358197
1550:25691137
1106:20929779
1098:18247345
982:27442443
873:12877193
735:See also
281:using ΔG
167:micelles
149:cysteine
122:entropic
93:methanol
2351:2741215
2300:5135335
2277:Bibcode
2198:8611495
2155:1823375
2147:8836100
2009:3945310
1981:Bibcode
1958:4839053
1915:3299367
1875:Bibcode
1742:7921179
1670:Bibcode
1619:Bibcode
1542:2331515
1454:1911756
1376:2394979
1368:1206727
1340:Bibcode
1308:7213619
1262:4023714
1234:Bibcode
1226:Science
1211:4338901
1175:Bibcode
1060:8347995
1017:6383201
973:5024328
933:7183857
905:Bibcode
798:7108955
171:polymer
109:entropy
2358:
2348:
2307:
2297:
2248:
2240:
2196:
2188:
2153:
2145:
2137:
2066:
2058:
2050:
2015:
2007:
1999:
1973:Nature
1956:
1948:
1913:
1906:305105
1903:
1895:
1846:
1810:
1775:
1740:
1732:
1696:
1688:
1645:
1637:
1596:994183
1594:
1586:
1548:
1540:
1532:
1488:
1452:
1444:
1409:
1374:
1366:
1358:
1306:
1298:
1260:
1252:
1209:
1203:763335
1201:
1193:
1167:Nature
1104:
1096:
1058:
1050:
1015:
980:
970:
931:
923:
871:
863:
796:
778:
572:−0.07
519:−0.71
516:−0.94
505:−0.02
502:−0.24
474:−0.01
452:−0.06
438:−0.24
435:−2.09
432:−1.85
424:−0.31
410:−0.44
407:−0.67
404:−0.23
396:−0.53
393:−0.46
382:−0.58
379:−1.71
376:−1.13
368:−0.69
365:−1.25
362:−0.56
354:−0.81
351:−1.12
348:−0.31
165:(SDS)
142:Expasy
97:hexane
2151:S2CID
2064:S2CID
2013:S2CID
1546:S2CID
1372:S2CID
1207:S2CID
1102:S2CID
662:2.41
659:3.64
656:1.23
653:Asp-
648:1.81
645:2.80
642:0.99
639:Lys+
634:1.61
631:3.63
628:2.02
625:Glu-
620:1.37
617:2.33
614:0.96
611:His+
606:1.14
603:1.15
600:0.01
592:1.00
589:1.81
586:0.81
583:Arg+
578:0.50
575:0.43
569:Asp0
564:0.43
561:0.85
558:0.42
550:0.33
547:0.46
544:0.13
536:0.33
533:0.50
530:0.17
522:0.23
508:0.22
494:0.19
491:0.77
488:0.58
480:0.12
477:0.11
471:Glu0
466:0.11
463:0.25
460:0.14
449:0.11
446:0.17
443:His0
421:0.14
418:0.45
390:0.07
85:water
2356:PMID
2305:PMID
2246:PMID
2238:ISSN
2194:PMID
2186:ISSN
2143:PMID
2135:ISSN
2056:PMID
2048:ISSN
2005:PMID
1997:ISSN
1954:PMID
1946:ISSN
1911:PMID
1893:ISSN
1844:ISSN
1808:ISSN
1773:ISSN
1738:PMID
1730:ISSN
1694:PMID
1686:ISSN
1643:PMID
1635:ISSN
1592:PMID
1584:ISSN
1538:PMID
1530:ISSN
1486:ISSN
1450:PMID
1442:ISSN
1407:ISSN
1364:PMID
1356:ISSN
1304:PMID
1296:ISSN
1258:PMID
1250:ISSN
1199:PMID
1191:ISSN
1120:link
1094:PMID
1056:PMID
1048:ISSN
1013:PMID
978:PMID
929:PMID
921:ISSN
869:PMID
861:ISSN
849:1000
794:PMID
597:Gly
555:Asn
541:Ser
527:Ala
513:Tyr
499:Cys
485:Gln
457:Thr
429:Trp
415:Pro
401:Met
387:Val
373:Phe
359:Leu
345:Ile
332:woct
320:woct
285:− ΔG
283:woct
120:and
2346:PMC
2336:doi
2332:106
2295:PMC
2285:doi
2273:113
2230:doi
2178:doi
2127:doi
2040:doi
1989:doi
1977:319
1938:doi
1934:161
1901:PMC
1883:doi
1836:doi
1832:803
1800:doi
1796:216
1765:doi
1722:doi
1718:676
1678:doi
1627:doi
1576:doi
1572:105
1522:doi
1478:doi
1474:240
1434:doi
1399:doi
1348:doi
1288:doi
1242:doi
1230:229
1183:doi
1171:277
1086:doi
1040:doi
1005:doi
968:PMC
960:doi
913:doi
853:doi
786:doi
772:157
339:wif
334:− Δ
308:wif
287:wif
50:of
38:of
34:or
2402::
2354:.
2344:.
2330:.
2326:.
2303:.
2293:.
2283:.
2271:.
2267:.
2244:.
2236:.
2226:28
2224:.
2192:.
2184:.
2174:35
2172:.
2149:.
2141:.
2133:.
2121:.
2085:^
2062:.
2054:.
2046:.
2036:42
2034:.
2011:.
2003:.
1995:.
1987:.
1975:.
1952:.
1944:.
1932:.
1909:.
1899:.
1891:.
1881:.
1871:84
1869:.
1865:.
1842:.
1830:.
1806:.
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