Proteins are molecules of great size, complexity, and diversity. They are the source of dietary amino acids, both essential and nonessential, that are used for growth, maintenance, and the general well-being of man. These macromolecules, characterized by their nitrogen contents, are involved in many vital processes intricately associated with all living matter. In mammals and many   internal organs are largely composed of proteins. Mineral matter of bone is held together by collagenous protein. Skin, the protective covering of the body, often accounts for about 10% of the total body protein.

    Some protein function as biocatalysts (enzymes and hormones) to regulate chemical reactions within the body. Fundamental life process, such as growth, digestion and metabolism, excretion, conversion of chemical energy into mechanical work, etc, are controlled by enzymes and hormones. Blood plasma proteins and hemoglobin regulate the osmotic pressure and PH of  certain body fluids. Proteins are necessary for immunology reactions. Antibodies, modified plasma globulin proteins, defend against the invasion of foreign substances of microorganisms that can cause various diseases, food allergies result when certain ingested proteins cause an apparent modification in the defense mechanism. This leads to a variety of painful, and occasionally drastic, conditions in certain individuals.

Food shortages exist in many areas of the world, and they are likely to

become more acute and widespread as the world’s population increases. providing

adequate supplies of protein poses a much greater problem than providing

adequate supplies of either carbohydrate or fat. Proteins not only are more

costly to produce than fats or carbohydrates but the daily protein requirement

per kilogram of bodyweight remains constant throughout adult life, whereas the

requirements for fats and carbohydrates generally decrease with age.

  As briefly described above, proteins have diverse biological functions, structures, and properties. Many proteins are susceptible to alteration by a number of rather subtle changes in the immediate environment. Maximum knowledge of the composition, structure, and chemical properties of the raw materials, especially proteins, is required if contemporary and future processing of foods is to best meet the needs of mankind. A considerable amount of information is already available, although much of it has been collected by biochemists using a specific food component as a model system,

      Amino Acids

 Amino acids are the “building blocks” of proteins. Therefore, to understand the properties of proteins, a discussion of the structures and properties o f amino acids is required. Amino acids are chemical compounds, which contain both basic amino groups and acidic carboxyl groups. Amino acids found in proteins have both the amino and carboxyl groups on the a-carbon atom; a-amino acids have the following general structure:

     At neutral pH values in aqueous solutions both the amino and the carboxyl groups are ionized. The carboxyl group loses a proton and obtains a negative charge, while the amino group gains a proton and hence acquires a positive charge. As a consequence, amino acids possess dipolar characteristics. The dipolar, or zwitterions, form of amino acids has the following general structure:

    Several properties of amino acids provide evidence for this structure: they are more soluble in water than in less polar solvents; when present in crystalline form they melt or decompose at relatively high temperatures (generally above 200): and they exhibit large dipole moments and large dielectric constants in neural aqueous solutions.

The R groups or side chains, of amino acids and proteins. these side chains may be classified in to four groups.

Amino acids with polar-uncharged (hydrophilic) r groups can hydrogenbond with water and are generally soluble in aqueous solutions. The hydroxyls of serine, heroine, and tyrosine; the sulfhydryl of thinly of cysteine, and the amides of asparagines and glutamine are the functional moieties present in r groups of the class of amino acids. Two of these, the toil of cysteine and the hydroxyl of tyrosine, are slightly ionized at PG 7 and can lose a proton much more readily than others in this class. The amides of asparagines and glutamine are readily hydrolyzed by acid or base to aspartic and glutamic acids, respectively.

Amino acids with nonpolar (hydrophobic) r groups are less soluble in aqueous solvents than amino acids with polar uncharged r groups. Five amino acids with hydrocarbon side chains decrease in polarity as the length of the side chain is increased. The unique structure of praline (and its hydoxylated derivative, hydroxyproline) causes this amino acid to play a unique role in protein structure.

The amino acids with positively charged (basic) r groups at ph 6-7 are lysine; argiine has a positively charged quanidino group. At ph 7.0 10% of the imidazole groups of histidine molecules are prorogated, but more than 50% carry positive at ph 6.0.

The dicarboxylic amino acids, asparic glutamic, possess net negative charges n the neutral ph range. An important artificial meal-flavoring food additive is the monosodium salt of glutamic acid.

Peptides

When the amino group of one amino acid reacts with the carboxyl group of another amino acid, a peptide bond is formed and a molecule of water is released. This can bond joins amino acids together to form proteins

The peptide bond is slightly shorter than otter single c-n bonds. This indicates that the peptide bond has some characteristics of a double bond, because of resonance stabilization with the carbony1 oxygen. Thus group adjacent to the peptide bond cannot rotate freely, this rigidity of the peptide bond holds

the six atoms in a single plane. the amino (_NH_) group does not ionize between ph o and 14 due to the double-bond properties of the peptide bond. In addition, r groups on amino acid residues, because of starch hindrance, force oxygen and hydrogen of the peptide bond to exist on a trans configuration. Therefore, the backbone of peptides and proteins has free rotation in two of the three bonds between amino acids.

If a few amino acids are joined together by peptide bonds the compound is called a” most natural peptides are formed by the partial hydrolytic of proteins; however, a few peptides are important metabolites. Ansetime and carnosine are two derivatives of histamine that are found in muscles pf animals. The biochemical function of these peptides is not understood.

  Glutathione occurs in mammalian blood, yeast, and especially in tissues of rapidly dividing cells. It is thought to function in oxidative metabolism and detoxification.

  Duirng oxidation, two moletcules of glutathiune join vin a disulfide bridge (-S-S) between two cysteine is not found in proteins.

  Other peptides functino as antibodies and hormones. Oxytocin and hormones. Oxytocin and vasopressin are examples of peptide hormones.

Protein structure 

Proteins perform a wide variety of biological functions and since they are composed of hundreds of amino acids, their structures are much mere complex than those of peptides.

Enzymes are globular proteins produced in living matter for the special purpose of catalyzing vital chemical reactions that otherwise do not occur under physiological conditions. Hemoglobin and myoglobin are hemo-containing proteins that transport oxygen and carbon dioxide in the blood and muscles. The major muscle proteins, actin and myosin, convert chemical energy to mechanical work, while proteins in tendons (collagen and elastim) bind muscles to bones, skin, hairy fingernails, and toenails are pertinacious protective substance.  The food scientist is concerned about proteins in foods since knowledge of protein structure and behavior allows him to more ably manipulate foods for the benefit mankind.

Nearly an infinite number of proteins could be synthesized from the 21natural occurring amino acids. However, it has been estimated that only about 2000 different proteins exist in nature.  The number is greater than this if one considers the slight variations found in proteins from different species.

The linear sequence of amino acids in protein is referred toast “primary structure “. In a few proteins the primary structure has been determined and one protein (ribonuclease) has been synthesized in the laboratory. It is the unique sequence of amino acids that imparts many of the fundamental properties to different protein and tertiary structures. If the protein contains a considerable number of amino acids with hydrophobic groups, its solubility in aqueous solvents is probable less than that of proteins containing amino acids with many hydrophilic groups.

If the primary structure of the protein were not folded, protein molecules would be excessively long and thin. A protein having a molecular weight of 13,000 would be 448 a thick. This structure allows excessive interaction with other substances, and it is not found in nature The three-dimensional manner in which relatively close members of the protein chain are arranged is referred to as” secondary structure.”

examples or secondary structure are the a-helix of wool, the pleated-sheet configuration of silk, and the collagen helix.

The native structure of a protein is that structure which possesses the lowest feasible free energy. Therefore, the structure of a protein is not random but somewhat ordered. when the restrictions of the peptide bond are superimposed on a polyamino acid chain of a globular protein, a right handed coil, the ∝-helix, appears to be one of the most ordered and stable structures feasible.  

the ∝-helix contains 3.6 amino acid residues per turn lof the protein backbone, with the r groups of the amino acids extending outward from the axis of the helical structure, hydrogen bonding can occur between the nitrogen of one peptide bond and the oxygen of another peptide bond four residues along the protein chain, the hydrogen bonds are nearly parallel to the axis of the helix, lending strength to the helical structure, since this arrangement allows each peptide bond to form a hydrogen bond, the stability of the structure greatly enhanced. The coil of the helix is sufficiently compact and stables that even substances with strong tendencies to participate in hydrogen bonding, such as water, cannot enter the core.

A secondary saturation found in many fibrous proteins is the β-pleated sheet configuration. In this configuration the peptide backbone forms a zigzag pattern, with the r groups of the amino acids extending alive and below the peptide chain. Since all peptide bonds are available for hydrogen bonding, this configuration allows maximum cross-linking between adjacent polypeptide chains and thus good stability. Both parallel-pleated sheet, where the polypeptide chains run in opposite directions, are possible. Where groups are bulky or have little charges, the interactions of the r groups do not allow the pleated-sheet configuration to exist. silk and insect fibers are the best examples of theβ-sheet, although feathers of birds contain a complicated form of these configuration.

Another type of secondary structure of fibrous proteins is the collagen helix. collagen is the most abundant protein in higher vertebrates, accounting for one-third of the total body protein, collagen resists stretching, is the major component of tendons, and contains one-third glycine and one-fourth proline or hydroxyprolinethe rigid r groups, and the lack of hydrogen bonding by peptide linkages involving proline and hydroxyproline, prevents formation of an ∝-helical structure and forces the collagen polypeptide chain into an odd kinked-type helix. Peptide bonds composed of glycine form interchain hydrogen bonds with two other collagen polypeptide chains, and this results in a stable triple helix. This triple-helical structure is called “tropocollagen” and it has a molecular weight of 3000,000 Daltons.

The manner in, which large portions of it protein chain are arranged is referred to as tertiary structure. This involves folding of regular unts of the secondary structure as well as the structuring of areas of the peptide chain that are devoid of secondary structure. for example, some proteins contain areas where ∝-helical structure exists and other areas where this structure cannot form. depending on the amino acid sequence, the length of the ∝-helical portions are held together by hydrogen bonds formed between r groups, by salt linkages, by hydrophobic interactions, and by covalent disulfide(-s-s-0 linkages.

The structures discussed so far have involved only a single peptide chain. The structure formed when individual (subunit) polypeptide chains interact to form a native protein molecule is referred to as “quaternary structure”. The bonding mechanisms that hold protein chains together are generally the same as those involved in tertiary structure, with the possible exception that disulfide bonds do not assist in maitaining the quaternary structures of proteins

 

第四課  氨基酸和蛋白質

    蛋白質錯綜復雜、多種多樣的大分子物質,是食物必須氨基酸和非必須氨基酸的來源。人體利用這些氨基酸以滿足生長發育、修復組織和維持正常健康生活的要求。這些大分子以含氮為其特征，參與了許多與各種有生命物質有復雜聯系的生命過程。在包括人類在內的哺乳動物中，蛋白質起著機體改造成分的作用，肌肉和許多體內器官主要由蛋白質構成。骨骼中的礦物質靠膠原蛋白得以保持在一起。機體的保護層—皮膚中的蛋白質通常占機體蛋白質總量的10%的左右。

    有些蛋白質有生物催化劑（酶和激素）的作用，以調節體內的化學反應。基本的生命過程如生長、消化、代謝、排泄、化學能轉變成機械功等等都受酶和激素的控制。某些體液的滲透壓和pH值受制于血漿蛋白和血紅蛋白。蛋白質對免疫反應是必不可少的。抗體（改性的血漿球蛋白能引起疾病的外來雜質和微生物的入侵。當某些攝入的蛋白質使防御機制產生明顯的變化時，便發生人體的生物過敏。這就導致某些個體身上出現各種各樣的疾病，且有時是急劇的病情。

    食物短缺現象在世界許多地區存在。隨著人口的增加，這個問題很可能愈來愈尖銳、愈普遍。而蛋白質供應不足問題遠比碳水化合物或脂肪供應不足更為嚴重。蛋白質不僅它的產出費用要比碳水化合物或脂肪的產出費用為高，而且每千克每天所需的蛋白質量造整個成年期是恒定的，而每天所需的脂肪和碳水化合物量一般都隨著年齡的增長而逐漸減少。

正如上面簡述的一樣，蛋白質有多種不同的結構、性質和生理功能。許多蛋白質容易受周圍環境的一系列微妙變化的影響而發生變化。要想使現在和將來的食品加工能理想的滿足人類的需要，就必須徹底了解原料特別是蛋白質的組成結構和化學性質。目前，已經有這方面的大量資料可供利用，不過其中大部分是生物化學家利用某一特定食物成分作為模擬物系加以收集的。

氨基酸

    氨基酸是蛋白質的“結構單元”。因此，要了解蛋白質的性質，舊需要討論氨基酸的結構和性質。氨基酸是既含氨基又含酸性羧基的化合物。蛋白質中的氨基酸在α-碳原子上同時有氨基和羧基。α-氨基酸具有如下的一般結構：

在中性pH水溶液中，氨基和羧基都呈離子狀態。羧基失去一個質子而帶負電荷，同時氨基得到一個質子而帶正電荷。結果氨基酸便具有偶極的特性。氨基酸的這種偶極形式（即兩性形式）有如下的一般結構：

氨基酸有好幾種性質都反映了這種結構，這些性質是：它們易溶于水而不易溶于極性很小的溶劑：當以晶體形式存在時，它們要在較高溫度（一般在200℃以上）下熔化或分解；它們在中性溶液種顯示出很大的偶極矩和介電常數。

    氨基酸的側鏈R基團對氨基酸和蛋白質的化學性質產生重大的影響。這些側鏈可以分為四類。

    帶有極性非荷電的（親水的）R基團的氨基酸能與水形成氫鍵，通常能溶于水溶液。絲氨酸、蘇氨酸和酪氨酸的羥基，半胱氨酸的硫氫基（即硫醇）以及天冬酰胺和谷氨酰胺的酰胺基時出現在這類氨基酸R基團中的功能部分，其中半胱氨酸的硫羥基和酪氨酸的羥基在pH7時能輕度離子化，因而比這類中其它氨基酸更容易失去質子。天冬酰胺和谷氨酰胺的酰胺基容易被酸和堿水解，分別形成天冬氨酸和谷氨酸。

    帶有非極性（疏水的）R集團的氨基酸在水溶液中的溶解性比帶有極性非荷電的R基團的氨基酸要小得多。帶有烴側鏈的五種氨基酸，其側鏈隨側鏈長度增加而降低。脯氨酸（以及其烴基衍生物羥脯氨酸）的獨特結構使這種氨基酸在蛋白質結構中有獨特的地位。

    pH6～7時帶正電荷（堿性的）R基團的氨基酸有賴氨酸、精氨酸和組氨酸。賴氨酸帶正電的原因主要在于氨基，而精氨酸則具有帶正電荷的胍基。pH7時組氨酸分子中的咪唑基有10%質子化，但在pH6時則有50%以上帶正電荷。

    二羥基氨基酸（天冬氨酸和谷氨酸）在中性pH范圍內帶凈負電荷，谷氨酸的一鈉鹽是一種重要的膳食調味用的人造食品添加劑。

肽

    當一個氨基酸分子的氨基與另一個氨基酸分子的羧基起反應時,便形成一個肽鍵，同時釋放出一分子水。這種C-N鍵把眾多的氨基酸連接在一起形成蛋白質。    

這種肽鍵比其它簡單的C-N鍵略短,這說明由于肽鍵與羰基氧的共振穩定作用，肽鍵具有了一定的雙鍵特性。這樣，緊鄰肽鍵的基團就不能自由轉動了。肽鍵的這種剛性使六個原子保持在一個平面上。      H

由于肽鍵的雙鍵性質，亞氨基（-NH-)在pH0～14之間均不能離子化。此外，由于立體位阻現象，氨基酸殘基上的R基團迫使肽鍵上的氧原子和氫原子只能以反式構型存在。因此，多肽和蛋白質的主鏈只可能在氨基酸之間的三個鍵中的兩個鍵上作自由轉動。

    如果少數幾個氨基酸以肽鍵連接起來，這樣的化合物就稱為“肽”大多數天然肽是由蛋白質部分水解形成的。可是，有少數肽則是重要的代謝產物。鵝肌肽和肌肽是動物肌肉中組氨酸的兩種衍生物，這些肽生物化學功能目前還不清楚。

    谷胱甘肽存在于哺乳動物血液、酵母之中，特別是快速分解的細胞質組織中。一般認為，這種肽具有參與氧化代謝和解毒作用的功能。氧化過程中，兩分子谷胱甘肽通過兩個半胱氨酸殘基之間的二硫鍵-S-S-連接起來。在蛋白質中未曾發現谷氨酸的γ-羰基與半胱氨酸連成的肽鍵。

此外，還有具抗體和激素功能的肽。催產素和抗利尿素就是肽激素的例子。

蛋白質的結構

    蛋白質執行的多種多樣的生物功能，而且由于它是數百個氨基酸組成的，故其結構遠比肽為復雜。

    酶是生物中產生的球狀蛋白質，目的是專門催化某些生物化學反應，不然的話，這些化學反應在生理條件下是不會發生的。血紅蛋白和肌紅蛋白是輸送血液和肌肉中氧和二氧化碳的含血紅素的蛋白質。重要的肌肉蛋白—肌動蛋白和肌球蛋白把化學能轉變成機械能；而腱中的蛋白質（膠原蛋白和彈性蛋白）則是將肌肉粘連在骨骼上。皮膚、毛發、指（趾）甲是蛋白質類的保護物質。食品科學家之所以關注食物蛋白質，是因為掌握了蛋白質結構和功能方面的知識，才能更好的加工和處理食品，造福于人類。

    用21種天然存在的氨基酸幾乎可以合成無數的蛋白質。可是，據估計自然界只存在約2000種不同的蛋白質，如果考慮不同物種蛋白質存在的微小差異，則蛋白質數目就超過此數。

    蛋白質分子內氨基酸的直線排列次序被看作是蛋白質的一級結構。少數蛋白質的一級結構已經被確定。而且已在實驗室里合成了其中一種蛋白質（核糖核酸）。正是這種氨基酸的獨特排列順序賦予不同蛋白質以許多基本特性，且在很大程度上決定了它們的二級和三級結構。如果蛋白質中含有大量帶疏水基團的氨基酸，則它在水溶劑中的溶解性就可能比帶許多親水基團的氨基酸的蛋白質差。

    如果蛋白質的一級結構不是折疊的，那么蛋白質分子就會很長很細。分子量為13,000蛋白質分子就應有448納米長和3.7納米粗這種結構將使它們可能與其它物質發生過度的相互反應，然而這樣的結構在自然界還未發現。蛋白質鏈中相互靠近的鏈節與鏈節之間的三維排列方式即為蛋白質的“二級結構”。二級結構的具體例子有羊毛蛋白的α-螺旋結構，蠶絲蛋白的折疊片結構和膠原蛋白的螺旋結構。

    蛋白質的自然結構是含有最低可能自由能的結構。因此，蛋白質的結構不是任意的，而是有一定規則的。當球狀蛋白質的聚氨基酸鏈上受到肽鍵約束時，右螺旋（即α-螺旋）看來是最有規則、最為穩定的合理結構之一。

    每一圈α-螺旋的蛋白質主鏈上含有3.6個氨基酸殘基，而氨基酸的R基團則從螺旋結構的軸線向外伸出，一個肽鍵的氮能夠與另一個沿蛋白質主鏈相距四個氨基酸殘基處的氧形成氫鍵。此氫鍵差不多與α-螺旋軸線平行，賦予螺旋結構以強度。由于這樣的排列能使每一個肽鍵都能形成氫鍵，因此大大加強了結構的穩定性。螺旋圈是非常緊密和堅固的，所以即使象水那樣的有強烈參與形成氫鍵趨勢的物質，也不能進入螺旋中央部分。

    出現在許多纖維狀蛋白質中的二級結構是β-折疊片結構。在這構型中，肽主鏈呈鋸齒形，其氨基酸的R基團向肽鏈的上方和下方伸展。由于所有肽鍵都可供氫鍵形成，故這種構型能夠使相鄰的多肽鏈之間充分形成交聯，從而具有良好的穩定性。有兩種折疊片，即相鄰多肽鏈走向相同的平行折疊片和走向相反的反平行折疊片，均有可能存在。如果多肽鏈中R基團過大，或帶有同種電荷，則R基團間的相互作用使β-折疊片不可能形成。蠶絲和昆蟲纖維蛋白是β-折疊結構的最好例子，而鳥類羽毛中所含的是這種構型的復雜形式。

    纖維蛋白的另一種二極結構是膠原螺旋。膠原螺旋是高等脊椎動物中最豐富的一種蛋白質，占動物體蛋白總量的1/3。膠原蛋白中含有1\3的甘氨酸和1\4脯氨酸或羥脯氨酸，能抵抗拉伸,是腱的主要組分。由于R基團的剛性以及脯氨酸、羥脯氨酸參與的肽式鍵合不能形成氫鍵的原因，所以α-螺旋結構無法形成，迫使膠原多肽鏈變成一種零散結節式的螺旋體，膠原多肽鏈中由甘氨酸構成的肽鍵與另兩條多肽鏈形成了鍵間氫鍵，產生了一種穩定的三股螺旋。此三股螺旋結構稱為“原膠原”，其分子量為30萬道爾頓。

    蛋白質鏈中大鏈段的排列方式稱為蛋白質的“三級結構”。它包括二級結構常規單元的折疊以及無二級結構肽鏈若干區域的結構化。例如，某些蛋白質中包含了有α-螺旋結構存在的區域和另外不能形成這種結構的區域。根據氨基酸順序的不同，此α-螺旋段的長度也不同，并賦予獨特的三級結構，這些折疊部分是靠R基團之間所形成的氫鍵，靠鹽鍵、疏水相互作用以及共價二硫鍵（-S-S-）而結合在一起的。

至此所討論的結構僅涉及單個肽鏈的結構。各個（亞單位）多肽鏈相互作用變成天然蛋白質分子時所形成的結構即為蛋白質的“四級結構”。使蛋白質鍵結合在一起的鍵合機制通常與三級結構中所述的相同，可能的例外情況是雙硫鍵不參與蛋白質四級結構的保持。

 

專業英語詞匯

 

 

intricate  a.復雜的,錯綜的,纏結的,難懂的

collagenous a.膠原的

globulin 球蛋白

plasma 血漿，原生質

immunological 免疫的

hemoglobin 血紅蛋白

basic amino 堿性的氨基

acidic carboxyl 酸性的羧基

aqueous ①水的 ②含水的 ③水成的

proton 質子,氕核

dipolar 偶極的,兩極的

zwitterion 兩性離子

crystalline ①結晶的,晶狀 ②清澈的

hydrophilic 親水的

serine 絲氨酸,羥基丙氨酸

threonine 羥基丁氨酸,蘇氨酸

tyrosine 酪氨酸, 3-對羥苯基丙氨酸

sulfhydryl 氫硫的  ～enzyme 硫化氫解酶  ～ group 巰基

cysteine 半胱氨酸,巰基丙氨酸

cystine 胱氨酸,雙巰丙氨酸

amide ①酰胺 ②氨化物

asparagine  天門冬酰胺

glutamine 谷氨酰胺

aspartic acid 天門冬氨酸,丁氨二酸

glutamic acid 谷氨酸

proline 脯氨酸,氮戊環-[2]-基羧酸

lysine 賴氨酸

arginine 精氨酸

histidine 組氨酸,咪唑丙氨酸

quanidino 胍

imidazol n. 咪唑;1,3-二氮雜茂

resonance n. ①回聲,反響 ②[物]共振,共鳴;諧振 ③[醫]叩響

imino 亞氨

steric a.空間的,位的

anserine 鵝肌肽

carnosine 肌肽

glutathione 谷胱甘肽

peptide肽,縮氨酸

oxytocin n.(垂體)后葉催產素

vasopressin n.后葉加(血)壓素,加壓素

carbonyl 羰基,碳酰

hemoglobin 血紅蛋白  hemo-表示“血”

myoglobin 肌紅蛋白

actin 肌動蛋白

myosin 肌球蛋白

tendon 腱,筋根

collagen 膠原,膠原蛋白

elastin 彈性蛋白

ribonuclease 核糖核酸酶

hydrophobic 疏水的

restriction n. 限制,限定,約束

vertebrate n.脊椎動物    a.①有椎骨的,有脊椎的,脊椎動物的 ②(作品等)結構嚴密的

kink n.①(繩索,頭發的)細結,絞纏 ②奇想,怪念頭,乖僻 ③(奇特的)妙法 ④(頸背等處的)

     肌肉痙攣,抽筋 ⑤[美](結構或設計等的)缺陷   vt.使紐結,使絞纏  vi紐結,打結

glycine 甘氨酸,氨基醋酸

tropocollagen 原膠原

dalton 道爾頓

devoid a. 缺乏,沒有(of)

covalent 共價    ～ bond共價鍵

quaternary a.①四個一組的,四部組成的,第四的 ②四元的,四價的,季的 ③[地]第四紀的

          n.①四,四個一組,第四組中的組成部分 ②[數]四進制 ③[地]第四紀

zigzag ①之字形，Z字形，鋸齒形；②之字形的線條（或道路、壕溝、裝飾等）；③蜿蜒曲折，盤旋彎曲

 

專業英語總結

 

English      Knowledge point:

 

1.       be of +名詞，相當于形容詞。

 

F： Proteins are molecules of great size, complexity, and diversity, proteins are molecules of great size, complexity, and diversity. roteins are molecules of great size, complexity, and diversity, proteins are molecules of great size, complexity, and diversity.

 

 

2.      at PH 7,  at neutral PH (用介詞at)

 

SOME GOOD SENTENCE:

 

1.       Amino acids are the “building blocks” of proteins.

Skin the protective covering of the body, often accounts for about 10% of the total body protein.

 

2.       Skin the protective covering of the body, often accounts for about 10% of the total body protein.

 

3.       Many proteins are susceptible to alteration by a number of rather subtle changes in the immediate environment.

 

4.       A considerable amount of information is already available, although much of it has been collected by biochemists using a specific food component as a model system.

 

5.       Several properties of amino acids provide evidence for this structure.

 

6.       The amino is responsible for the positive charge of lysine .while arginine has a positively charged quanidino group.

 

 

English      Knowledge point:

 

1.       be of +名詞，相當于形容詞。

 

F： Proteins are molecules of great size, complexity, and diversity, proteins are molecules of great size, complexity, and diversity. roteins are molecules of great size, complexity, and diversity, proteins are molecules of great size, complexity, and diversity.

 

 

2.      at PH 7,  at neutral PH (用介詞at)

 

 

專業英語難點

 

SOME GOOD SENTENCE:

 

1.       Amino acids are the “building blocks” of proteins.

Skin the protective covering of the body, often accounts for about 10% of the total body protein.

 

2.       Skin the protective covering of the body, often accounts for about 10% of the total body protein.

 

3.       Many proteins are susceptible to alteration by a number of rather subtle changes in the immediate environment.

 

4.       A considerable amount of information is already available, although much of it has been collected by biochemists using a specific food component as a model system.

 

5.       Several properties of amino acids provide evidence for this structure.

 

6.       The amino is responsible for the positive charge of lysine .while arginine has a positively charged quanidino group.